Voltammetric studies on the interaction of orange G with proteins: analytical applications

The interaction of orange G with protein was investigated by voltammetric method in this paper. In pH 2.0 Britton-Robinson (B-R) buffer solution orange G displayed an irreversible voltammetric reduction peak at -0.17 V (vs. SCE) on mercury working electrode. The addition of human serum albumin (HSA) into the orange G solution resulted in the decrease of the reduction current peak apparently without the changes of peak potentials and no new peaks appeared. The electrochemical parameters of orange G solution in the absence and presence of HSA were calculated and compared. The results showed that there were no significant changes, which indicated that the electrochemical behaviors of reaction solution on the mercury working electrode showed no changes and a supramolecular electrochemical inactive biocomplex was formed. The interaction mechanism was due to the formation of the microelectrostatic field in albumin structure in aqueous solution and caused the interaction with orange G, which induced the decrease of the equilibrium concentration of orange G in the reaction solution, and the decrease of the reductive peak current. The interaction conditions were discussed carefully. Under the optimal conditions the decrease of peak current was proportional to the concentration of protein and further used to the determination of different kinds of proteins. The calibration curves for the determination of HSA, bovine serum albumin (BSA), ovalbumin (OVA), bovine hemoglobin (BHb), lipase were linear over the ranges of 4.0~28.0 mg L-1, 4.0~30.0 mg L-1, 2.0~20.0 mg L-1, 2.0~25.0 mg L-1, 2.0~30.0 mg L-1, respectively. The detection limit was 3.0 mg L-1 for HSA, 3.5 mg L-1 for BSA, 1.0 mg L-1 for OVA, BHb and lipase. The new established electrochemical method was applied to determine the content of albumin in healthy human serum samples and the results were in good agreement with the traditional Coomassie Brilliant Blue (GBB G-250) spectrophotometric method. Ausführliche Beschreibung

Gespeichert in:

Autor*in:	Sun Wei [verfasserIn] Han Junying [verfasserIn] Ren Yong [verfasserIn] Jiao Kui [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2006

Schlagwörter:	orange G human serum albumin voltammetry interaction supramolecule

Übergeordnetes Werk:	In: Journal of the Brazilian Chemical Society - Sociedade Brasileira de Química, 2017, 17(2006), 3, Seite 510-517
Übergeordnetes Werk:	volume:17 ; year:2006 ; number:3 ; pages:510-517

Links:	Link aufrufen Link aufrufen Journal toc Journal toc

Katalog-ID:	DOAJ078292662

Internformat


LEADER	01000caa a22002652 4500
001	DOAJ078292662
003	DE-627
005	20230309155812.0
007	cr uuu---uuuuu
008	230228s2006 xx \|\|\|\|\|o 00\| \|\|eng c
035			\|a (DE-627)DOAJ078292662
035			\|a (DE-599)DOAJda500cb5b88b4ff4af27e9d27a17f97d
040			\|a DE-627 \|b ger \|c DE-627 \|e rakwb
041			\|a eng
050		0	\|a QD1-999
100	0		\|a Sun Wei \|e verfasserin \|4 aut
245	1	0	\|a Voltammetric studies on the interaction of orange G with proteins: analytical applications
264		1	\|c 2006
336			\|a Text \|b txt \|2 rdacontent
337			\|a Computermedien \|b c \|2 rdamedia
338			\|a Online-Ressource \|b cr \|2 rdacarrier
520			\|a The interaction of orange G with protein was investigated by voltammetric method in this paper. In pH 2.0 Britton-Robinson (B-R) buffer solution orange G displayed an irreversible voltammetric reduction peak at -0.17 V (vs. SCE) on mercury working electrode. The addition of human serum albumin (HSA) into the orange G solution resulted in the decrease of the reduction current peak apparently without the changes of peak potentials and no new peaks appeared. The electrochemical parameters of orange G solution in the absence and presence of HSA were calculated and compared. The results showed that there were no significant changes, which indicated that the electrochemical behaviors of reaction solution on the mercury working electrode showed no changes and a supramolecular electrochemical inactive biocomplex was formed. The interaction mechanism was due to the formation of the microelectrostatic field in albumin structure in aqueous solution and caused the interaction with orange G, which induced the decrease of the equilibrium concentration of orange G in the reaction solution, and the decrease of the reductive peak current. The interaction conditions were discussed carefully. Under the optimal conditions the decrease of peak current was proportional to the concentration of protein and further used to the determination of different kinds of proteins. The calibration curves for the determination of HSA, bovine serum albumin (BSA), ovalbumin (OVA), bovine hemoglobin (BHb), lipase were linear over the ranges of 4.0~28.0 mg L-1, 4.0~30.0 mg L-1, 2.0~20.0 mg L-1, 2.0~25.0 mg L-1, 2.0~30.0 mg L-1, respectively. The detection limit was 3.0 mg L-1 for HSA, 3.5 mg L-1 for BSA, 1.0 mg L-1 for OVA, BHb and lipase. The new established electrochemical method was applied to determine the content of albumin in healthy human serum samples and the results were in good agreement with the traditional Coomassie Brilliant Blue (GBB G-250) spectrophotometric method.
650		4	\|a orange G
650		4	\|a human serum albumin
650		4	\|a voltammetry
650		4	\|a interaction
650		4	\|a supramolecule
653		0	\|a Chemistry
700	0		\|a Han Junying \|e verfasserin \|4 aut
700	0		\|a Ren Yong \|e verfasserin \|4 aut
700	0		\|a Jiao Kui \|e verfasserin \|4 aut
773	0	8	\|i In \|t Journal of the Brazilian Chemical Society \|d Sociedade Brasileira de Química, 2017 \|g 17(2006), 3, Seite 510-517 \|w (DE-627)32461330X \|w (DE-600)2028738-0 \|x 16784790 \|7 nnns
773	1	8	\|g volume:17 \|g year:2006 \|g number:3 \|g pages:510-517
856	4	0	\|u https://doaj.org/article/da500cb5b88b4ff4af27e9d27a17f97d \|z kostenfrei
856	4	0	\|u http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532006000300012 \|z kostenfrei
856	4	2	\|u https://doaj.org/toc/0103-5053 \|y Journal toc \|z kostenfrei
856	4	2	\|u https://doaj.org/toc/1678-4790 \|y Journal toc \|z kostenfrei
912			\|a GBV_USEFLAG_A
912			\|a SYSFLAG_A
912			\|a GBV_DOAJ
912			\|a GBV_ILN_20
912			\|a GBV_ILN_22
912			\|a GBV_ILN_23
912			\|a GBV_ILN_24
912			\|a GBV_ILN_39
912			\|a GBV_ILN_40
912			\|a GBV_ILN_60
912			\|a GBV_ILN_62
912			\|a GBV_ILN_63
912			\|a GBV_ILN_65
912			\|a GBV_ILN_69
912			\|a GBV_ILN_70
912			\|a GBV_ILN_73
912			\|a GBV_ILN_95
912			\|a GBV_ILN_105
912			\|a GBV_ILN_110
912			\|a GBV_ILN_151
912			\|a GBV_ILN_161
912			\|a GBV_ILN_170
912			\|a GBV_ILN_213
912			\|a GBV_ILN_230
912			\|a GBV_ILN_285
912			\|a GBV_ILN_293
912			\|a GBV_ILN_602
912			\|a GBV_ILN_2014
912			\|a GBV_ILN_4012
912			\|a GBV_ILN_4037
912			\|a GBV_ILN_4112
912			\|a GBV_ILN_4125
912			\|a GBV_ILN_4126
912			\|a GBV_ILN_4249
912			\|a GBV_ILN_4305
912			\|a GBV_ILN_4306
912			\|a GBV_ILN_4307
912			\|a GBV_ILN_4313
912			\|a GBV_ILN_4322
912			\|a GBV_ILN_4323
912			\|a GBV_ILN_4324
912			\|a GBV_ILN_4325
912			\|a GBV_ILN_4338
912			\|a GBV_ILN_4367
912			\|a GBV_ILN_4700
951			\|a AR
952			\|d 17 \|j 2006 \|e 3 \|h 510-517

Indexfelder

author_variant	s w sw h j hj r y ry j k jk
matchkey_str	article:16784790:2006----::otmerctdeoteneatoooaggihrtis
hierarchy_sort_str	2006
callnumber-subject-code	QD
publishDate	2006
allfields	(DE-627)DOAJ078292662 (DE-599)DOAJda500cb5b88b4ff4af27e9d27a17f97d DE-627 ger DE-627 rakwb eng QD1-999 Sun Wei verfasserin aut Voltammetric studies on the interaction of orange G with proteins: analytical applications 2006 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The interaction of orange G with protein was investigated by voltammetric method in this paper. In pH 2.0 Britton-Robinson (B-R) buffer solution orange G displayed an irreversible voltammetric reduction peak at -0.17 V (vs. SCE) on mercury working electrode. The addition of human serum albumin (HSA) into the orange G solution resulted in the decrease of the reduction current peak apparently without the changes of peak potentials and no new peaks appeared. The electrochemical parameters of orange G solution in the absence and presence of HSA were calculated and compared. The results showed that there were no significant changes, which indicated that the electrochemical behaviors of reaction solution on the mercury working electrode showed no changes and a supramolecular electrochemical inactive biocomplex was formed. The interaction mechanism was due to the formation of the microelectrostatic field in albumin structure in aqueous solution and caused the interaction with orange G, which induced the decrease of the equilibrium concentration of orange G in the reaction solution, and the decrease of the reductive peak current. The interaction conditions were discussed carefully. Under the optimal conditions the decrease of peak current was proportional to the concentration of protein and further used to the determination of different kinds of proteins. The calibration curves for the determination of HSA, bovine serum albumin (BSA), ovalbumin (OVA), bovine hemoglobin (BHb), lipase were linear over the ranges of 4.0~28.0 mg L-1, 4.0~30.0 mg L-1, 2.0~20.0 mg L-1, 2.0~25.0 mg L-1, 2.0~30.0 mg L-1, respectively. The detection limit was 3.0 mg L-1 for HSA, 3.5 mg L-1 for BSA, 1.0 mg L-1 for OVA, BHb and lipase. The new established electrochemical method was applied to determine the content of albumin in healthy human serum samples and the results were in good agreement with the traditional Coomassie Brilliant Blue (GBB G-250) spectrophotometric method. orange G human serum albumin voltammetry interaction supramolecule Chemistry Han Junying verfasserin aut Ren Yong verfasserin aut Jiao Kui verfasserin aut In Journal of the Brazilian Chemical Society Sociedade Brasileira de Química, 2017 17(2006), 3, Seite 510-517 (DE-627)32461330X (DE-600)2028738-0 16784790 nnns volume:17 year:2006 number:3 pages:510-517 https://doaj.org/article/da500cb5b88b4ff4af27e9d27a17f97d kostenfrei http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532006000300012 kostenfrei https://doaj.org/toc/0103-5053 Journal toc kostenfrei https://doaj.org/toc/1678-4790 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 17 2006 3 510-517
spelling	(DE-627)DOAJ078292662 (DE-599)DOAJda500cb5b88b4ff4af27e9d27a17f97d DE-627 ger DE-627 rakwb eng QD1-999 Sun Wei verfasserin aut Voltammetric studies on the interaction of orange G with proteins: analytical applications 2006 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The interaction of orange G with protein was investigated by voltammetric method in this paper. In pH 2.0 Britton-Robinson (B-R) buffer solution orange G displayed an irreversible voltammetric reduction peak at -0.17 V (vs. SCE) on mercury working electrode. The addition of human serum albumin (HSA) into the orange G solution resulted in the decrease of the reduction current peak apparently without the changes of peak potentials and no new peaks appeared. The electrochemical parameters of orange G solution in the absence and presence of HSA were calculated and compared. The results showed that there were no significant changes, which indicated that the electrochemical behaviors of reaction solution on the mercury working electrode showed no changes and a supramolecular electrochemical inactive biocomplex was formed. The interaction mechanism was due to the formation of the microelectrostatic field in albumin structure in aqueous solution and caused the interaction with orange G, which induced the decrease of the equilibrium concentration of orange G in the reaction solution, and the decrease of the reductive peak current. The interaction conditions were discussed carefully. Under the optimal conditions the decrease of peak current was proportional to the concentration of protein and further used to the determination of different kinds of proteins. The calibration curves for the determination of HSA, bovine serum albumin (BSA), ovalbumin (OVA), bovine hemoglobin (BHb), lipase were linear over the ranges of 4.0~28.0 mg L-1, 4.0~30.0 mg L-1, 2.0~20.0 mg L-1, 2.0~25.0 mg L-1, 2.0~30.0 mg L-1, respectively. The detection limit was 3.0 mg L-1 for HSA, 3.5 mg L-1 for BSA, 1.0 mg L-1 for OVA, BHb and lipase. The new established electrochemical method was applied to determine the content of albumin in healthy human serum samples and the results were in good agreement with the traditional Coomassie Brilliant Blue (GBB G-250) spectrophotometric method. orange G human serum albumin voltammetry interaction supramolecule Chemistry Han Junying verfasserin aut Ren Yong verfasserin aut Jiao Kui verfasserin aut In Journal of the Brazilian Chemical Society Sociedade Brasileira de Química, 2017 17(2006), 3, Seite 510-517 (DE-627)32461330X (DE-600)2028738-0 16784790 nnns volume:17 year:2006 number:3 pages:510-517 https://doaj.org/article/da500cb5b88b4ff4af27e9d27a17f97d kostenfrei http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532006000300012 kostenfrei https://doaj.org/toc/0103-5053 Journal toc kostenfrei https://doaj.org/toc/1678-4790 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 17 2006 3 510-517
allfields_unstemmed	(DE-627)DOAJ078292662 (DE-599)DOAJda500cb5b88b4ff4af27e9d27a17f97d DE-627 ger DE-627 rakwb eng QD1-999 Sun Wei verfasserin aut Voltammetric studies on the interaction of orange G with proteins: analytical applications 2006 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The interaction of orange G with protein was investigated by voltammetric method in this paper. In pH 2.0 Britton-Robinson (B-R) buffer solution orange G displayed an irreversible voltammetric reduction peak at -0.17 V (vs. SCE) on mercury working electrode. The addition of human serum albumin (HSA) into the orange G solution resulted in the decrease of the reduction current peak apparently without the changes of peak potentials and no new peaks appeared. The electrochemical parameters of orange G solution in the absence and presence of HSA were calculated and compared. The results showed that there were no significant changes, which indicated that the electrochemical behaviors of reaction solution on the mercury working electrode showed no changes and a supramolecular electrochemical inactive biocomplex was formed. The interaction mechanism was due to the formation of the microelectrostatic field in albumin structure in aqueous solution and caused the interaction with orange G, which induced the decrease of the equilibrium concentration of orange G in the reaction solution, and the decrease of the reductive peak current. The interaction conditions were discussed carefully. Under the optimal conditions the decrease of peak current was proportional to the concentration of protein and further used to the determination of different kinds of proteins. The calibration curves for the determination of HSA, bovine serum albumin (BSA), ovalbumin (OVA), bovine hemoglobin (BHb), lipase were linear over the ranges of 4.0~28.0 mg L-1, 4.0~30.0 mg L-1, 2.0~20.0 mg L-1, 2.0~25.0 mg L-1, 2.0~30.0 mg L-1, respectively. The detection limit was 3.0 mg L-1 for HSA, 3.5 mg L-1 for BSA, 1.0 mg L-1 for OVA, BHb and lipase. The new established electrochemical method was applied to determine the content of albumin in healthy human serum samples and the results were in good agreement with the traditional Coomassie Brilliant Blue (GBB G-250) spectrophotometric method. orange G human serum albumin voltammetry interaction supramolecule Chemistry Han Junying verfasserin aut Ren Yong verfasserin aut Jiao Kui verfasserin aut In Journal of the Brazilian Chemical Society Sociedade Brasileira de Química, 2017 17(2006), 3, Seite 510-517 (DE-627)32461330X (DE-600)2028738-0 16784790 nnns volume:17 year:2006 number:3 pages:510-517 https://doaj.org/article/da500cb5b88b4ff4af27e9d27a17f97d kostenfrei http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532006000300012 kostenfrei https://doaj.org/toc/0103-5053 Journal toc kostenfrei https://doaj.org/toc/1678-4790 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 17 2006 3 510-517
allfieldsGer	(DE-627)DOAJ078292662 (DE-599)DOAJda500cb5b88b4ff4af27e9d27a17f97d DE-627 ger DE-627 rakwb eng QD1-999 Sun Wei verfasserin aut Voltammetric studies on the interaction of orange G with proteins: analytical applications 2006 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The interaction of orange G with protein was investigated by voltammetric method in this paper. In pH 2.0 Britton-Robinson (B-R) buffer solution orange G displayed an irreversible voltammetric reduction peak at -0.17 V (vs. SCE) on mercury working electrode. The addition of human serum albumin (HSA) into the orange G solution resulted in the decrease of the reduction current peak apparently without the changes of peak potentials and no new peaks appeared. The electrochemical parameters of orange G solution in the absence and presence of HSA were calculated and compared. The results showed that there were no significant changes, which indicated that the electrochemical behaviors of reaction solution on the mercury working electrode showed no changes and a supramolecular electrochemical inactive biocomplex was formed. The interaction mechanism was due to the formation of the microelectrostatic field in albumin structure in aqueous solution and caused the interaction with orange G, which induced the decrease of the equilibrium concentration of orange G in the reaction solution, and the decrease of the reductive peak current. The interaction conditions were discussed carefully. Under the optimal conditions the decrease of peak current was proportional to the concentration of protein and further used to the determination of different kinds of proteins. The calibration curves for the determination of HSA, bovine serum albumin (BSA), ovalbumin (OVA), bovine hemoglobin (BHb), lipase were linear over the ranges of 4.0~28.0 mg L-1, 4.0~30.0 mg L-1, 2.0~20.0 mg L-1, 2.0~25.0 mg L-1, 2.0~30.0 mg L-1, respectively. The detection limit was 3.0 mg L-1 for HSA, 3.5 mg L-1 for BSA, 1.0 mg L-1 for OVA, BHb and lipase. The new established electrochemical method was applied to determine the content of albumin in healthy human serum samples and the results were in good agreement with the traditional Coomassie Brilliant Blue (GBB G-250) spectrophotometric method. orange G human serum albumin voltammetry interaction supramolecule Chemistry Han Junying verfasserin aut Ren Yong verfasserin aut Jiao Kui verfasserin aut In Journal of the Brazilian Chemical Society Sociedade Brasileira de Química, 2017 17(2006), 3, Seite 510-517 (DE-627)32461330X (DE-600)2028738-0 16784790 nnns volume:17 year:2006 number:3 pages:510-517 https://doaj.org/article/da500cb5b88b4ff4af27e9d27a17f97d kostenfrei http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532006000300012 kostenfrei https://doaj.org/toc/0103-5053 Journal toc kostenfrei https://doaj.org/toc/1678-4790 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 17 2006 3 510-517
allfieldsSound	(DE-627)DOAJ078292662 (DE-599)DOAJda500cb5b88b4ff4af27e9d27a17f97d DE-627 ger DE-627 rakwb eng QD1-999 Sun Wei verfasserin aut Voltammetric studies on the interaction of orange G with proteins: analytical applications 2006 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The interaction of orange G with protein was investigated by voltammetric method in this paper. In pH 2.0 Britton-Robinson (B-R) buffer solution orange G displayed an irreversible voltammetric reduction peak at -0.17 V (vs. SCE) on mercury working electrode. The addition of human serum albumin (HSA) into the orange G solution resulted in the decrease of the reduction current peak apparently without the changes of peak potentials and no new peaks appeared. The electrochemical parameters of orange G solution in the absence and presence of HSA were calculated and compared. The results showed that there were no significant changes, which indicated that the electrochemical behaviors of reaction solution on the mercury working electrode showed no changes and a supramolecular electrochemical inactive biocomplex was formed. The interaction mechanism was due to the formation of the microelectrostatic field in albumin structure in aqueous solution and caused the interaction with orange G, which induced the decrease of the equilibrium concentration of orange G in the reaction solution, and the decrease of the reductive peak current. The interaction conditions were discussed carefully. Under the optimal conditions the decrease of peak current was proportional to the concentration of protein and further used to the determination of different kinds of proteins. The calibration curves for the determination of HSA, bovine serum albumin (BSA), ovalbumin (OVA), bovine hemoglobin (BHb), lipase were linear over the ranges of 4.0~28.0 mg L-1, 4.0~30.0 mg L-1, 2.0~20.0 mg L-1, 2.0~25.0 mg L-1, 2.0~30.0 mg L-1, respectively. The detection limit was 3.0 mg L-1 for HSA, 3.5 mg L-1 for BSA, 1.0 mg L-1 for OVA, BHb and lipase. The new established electrochemical method was applied to determine the content of albumin in healthy human serum samples and the results were in good agreement with the traditional Coomassie Brilliant Blue (GBB G-250) spectrophotometric method. orange G human serum albumin voltammetry interaction supramolecule Chemistry Han Junying verfasserin aut Ren Yong verfasserin aut Jiao Kui verfasserin aut In Journal of the Brazilian Chemical Society Sociedade Brasileira de Química, 2017 17(2006), 3, Seite 510-517 (DE-627)32461330X (DE-600)2028738-0 16784790 nnns volume:17 year:2006 number:3 pages:510-517 https://doaj.org/article/da500cb5b88b4ff4af27e9d27a17f97d kostenfrei http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532006000300012 kostenfrei https://doaj.org/toc/0103-5053 Journal toc kostenfrei https://doaj.org/toc/1678-4790 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 17 2006 3 510-517
language	English
source	In Journal of the Brazilian Chemical Society 17(2006), 3, Seite 510-517 volume:17 year:2006 number:3 pages:510-517
sourceStr	In Journal of the Brazilian Chemical Society 17(2006), 3, Seite 510-517 volume:17 year:2006 number:3 pages:510-517
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	orange G human serum albumin voltammetry interaction supramolecule Chemistry
isfreeaccess_bool	true
container_title	Journal of the Brazilian Chemical Society
authorswithroles_txt_mv	Sun Wei @@aut@@ Han Junying @@aut@@ Ren Yong @@aut@@ Jiao Kui @@aut@@
publishDateDaySort_date	2006-01-01T00:00:00Z
hierarchy_top_id	32461330X
id	DOAJ078292662
language_de	englisch
fullrecord	<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">DOAJ078292662</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230309155812.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">230228s2006 xx \|\|\|\|\|o 00\| \|\|eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)DOAJ078292662</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)DOAJda500cb5b88b4ff4af27e9d27a17f97d</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="050" ind1=" " ind2="0"><subfield code="a">QD1-999</subfield></datafield><datafield tag="100" ind1="0" ind2=" "><subfield code="a">Sun Wei</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Voltammetric studies on the interaction of orange G with proteins: analytical applications</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2006</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">Computermedien</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">The interaction of orange G with protein was investigated by voltammetric method in this paper. In pH 2.0 Britton-Robinson (B-R) buffer solution orange G displayed an irreversible voltammetric reduction peak at -0.17 V (vs. SCE) on mercury working electrode. The addition of human serum albumin (HSA) into the orange G solution resulted in the decrease of the reduction current peak apparently without the changes of peak potentials and no new peaks appeared. The electrochemical parameters of orange G solution in the absence and presence of HSA were calculated and compared. The results showed that there were no significant changes, which indicated that the electrochemical behaviors of reaction solution on the mercury working electrode showed no changes and a supramolecular electrochemical inactive biocomplex was formed. The interaction mechanism was due to the formation of the microelectrostatic field in albumin structure in aqueous solution and caused the interaction with orange G, which induced the decrease of the equilibrium concentration of orange G in the reaction solution, and the decrease of the reductive peak current. The interaction conditions were discussed carefully. Under the optimal conditions the decrease of peak current was proportional to the concentration of protein and further used to the determination of different kinds of proteins. The calibration curves for the determination of HSA, bovine serum albumin (BSA), ovalbumin (OVA), bovine hemoglobin (BHb), lipase were linear over the ranges of 4.0~28.0 mg L-1, 4.0~30.0 mg L-1, 2.0~20.0 mg L-1, 2.0~25.0 mg L-1, 2.0~30.0 mg L-1, respectively. The detection limit was 3.0 mg L-1 for HSA, 3.5 mg L-1 for BSA, 1.0 mg L-1 for OVA, BHb and lipase. The new established electrochemical method was applied to determine the content of albumin in healthy human serum samples and the results were in good agreement with the traditional Coomassie Brilliant Blue (GBB G-250) spectrophotometric method.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">orange G</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">human serum albumin</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">voltammetry</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">interaction</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">supramolecule</subfield></datafield><datafield tag="653" ind1=" " ind2="0"><subfield code="a">Chemistry</subfield></datafield><datafield tag="700" ind1="0" ind2=" "><subfield code="a">Han Junying</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="0" ind2=" "><subfield code="a">Ren Yong</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="0" ind2=" "><subfield code="a">Jiao Kui</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">In</subfield><subfield code="t">Journal of the Brazilian Chemical Society</subfield><subfield code="d">Sociedade Brasileira de Química, 2017</subfield><subfield code="g">17(2006), 3, Seite 510-517</subfield><subfield code="w">(DE-627)32461330X</subfield><subfield code="w">(DE-600)2028738-0</subfield><subfield code="x">16784790</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:17</subfield><subfield code="g">year:2006</subfield><subfield code="g">number:3</subfield><subfield code="g">pages:510-517</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">https://doaj.org/article/da500cb5b88b4ff4af27e9d27a17f97d</subfield><subfield code="z">kostenfrei</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532006000300012</subfield><subfield code="z">kostenfrei</subfield></datafield><datafield tag="856" ind1="4" ind2="2"><subfield code="u">https://doaj.org/toc/0103-5053</subfield><subfield code="y">Journal toc</subfield><subfield code="z">kostenfrei</subfield></datafield><datafield tag="856" ind1="4" ind2="2"><subfield code="u">https://doaj.org/toc/1678-4790</subfield><subfield code="y">Journal toc</subfield><subfield code="z">kostenfrei</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SYSFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_DOAJ</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_20</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_22</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_23</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_24</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_39</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_40</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_60</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_62</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_63</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_65</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_69</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_70</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_73</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_95</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_105</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_110</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_151</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_161</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_170</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_213</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_230</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_285</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_293</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_602</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2014</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4012</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4037</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4112</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4125</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4126</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4249</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4305</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4306</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4307</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4313</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4322</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4323</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4324</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4325</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4338</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4367</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4700</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">17</subfield><subfield code="j">2006</subfield><subfield code="e">3</subfield><subfield code="h">510-517</subfield></datafield></record></collection>
callnumber-first	Q - Science
author	Sun Wei
spellingShingle	Sun Wei misc QD1-999 misc orange G misc human serum albumin misc voltammetry misc interaction misc supramolecule misc Chemistry Voltammetric studies on the interaction of orange G with proteins: analytical applications
authorStr	Sun Wei
ppnlink_with_tag_str_mv	@@773@@(DE-627)32461330X
format	electronic Article
delete_txt_mv	keep
author_role	aut aut aut aut
collection	DOAJ
remote_str	true
callnumber-label	QD1-999
illustrated	Not Illustrated
issn	16784790
topic_title	QD1-999 Voltammetric studies on the interaction of orange G with proteins: analytical applications orange G human serum albumin voltammetry interaction supramolecule
topic	misc QD1-999 misc orange G misc human serum albumin misc voltammetry misc interaction misc supramolecule misc Chemistry
topic_unstemmed	misc QD1-999 misc orange G misc human serum albumin misc voltammetry misc interaction misc supramolecule misc Chemistry
topic_browse	misc QD1-999 misc orange G misc human serum albumin misc voltammetry misc interaction misc supramolecule misc Chemistry
format_facet	Elektronische Aufsätze Aufsätze Elektronische Ressource
format_main_str_mv	Text Zeitschrift/Artikel
carriertype_str_mv	cr
hierarchy_parent_title	Journal of the Brazilian Chemical Society
hierarchy_parent_id	32461330X
hierarchy_top_title	Journal of the Brazilian Chemical Society
isfreeaccess_txt	true
familylinks_str_mv	(DE-627)32461330X (DE-600)2028738-0
title	Voltammetric studies on the interaction of orange G with proteins: analytical applications
ctrlnum	(DE-627)DOAJ078292662 (DE-599)DOAJda500cb5b88b4ff4af27e9d27a17f97d
title_full	Voltammetric studies on the interaction of orange G with proteins: analytical applications
author_sort	Sun Wei
journal	Journal of the Brazilian Chemical Society
journalStr	Journal of the Brazilian Chemical Society
callnumber-first-code	Q
lang_code	eng
isOA_bool	true
recordtype	marc
publishDateSort	2006
contenttype_str_mv	txt
container_start_page	510
author_browse	Sun Wei Han Junying Ren Yong Jiao Kui
container_volume	17
class	QD1-999
format_se	Elektronische Aufsätze
author-letter	Sun Wei
author2-role	verfasserin
title_sort	voltammetric studies on the interaction of orange g with proteins: analytical applications
callnumber	QD1-999
title_auth	Voltammetric studies on the interaction of orange G with proteins: analytical applications
abstract	The interaction of orange G with protein was investigated by voltammetric method in this paper. In pH 2.0 Britton-Robinson (B-R) buffer solution orange G displayed an irreversible voltammetric reduction peak at -0.17 V (vs. SCE) on mercury working electrode. The addition of human serum albumin (HSA) into the orange G solution resulted in the decrease of the reduction current peak apparently without the changes of peak potentials and no new peaks appeared. The electrochemical parameters of orange G solution in the absence and presence of HSA were calculated and compared. The results showed that there were no significant changes, which indicated that the electrochemical behaviors of reaction solution on the mercury working electrode showed no changes and a supramolecular electrochemical inactive biocomplex was formed. The interaction mechanism was due to the formation of the microelectrostatic field in albumin structure in aqueous solution and caused the interaction with orange G, which induced the decrease of the equilibrium concentration of orange G in the reaction solution, and the decrease of the reductive peak current. The interaction conditions were discussed carefully. Under the optimal conditions the decrease of peak current was proportional to the concentration of protein and further used to the determination of different kinds of proteins. The calibration curves for the determination of HSA, bovine serum albumin (BSA), ovalbumin (OVA), bovine hemoglobin (BHb), lipase were linear over the ranges of 4.0~28.0 mg L-1, 4.0~30.0 mg L-1, 2.0~20.0 mg L-1, 2.0~25.0 mg L-1, 2.0~30.0 mg L-1, respectively. The detection limit was 3.0 mg L-1 for HSA, 3.5 mg L-1 for BSA, 1.0 mg L-1 for OVA, BHb and lipase. The new established electrochemical method was applied to determine the content of albumin in healthy human serum samples and the results were in good agreement with the traditional Coomassie Brilliant Blue (GBB G-250) spectrophotometric method.
abstractGer	The interaction of orange G with protein was investigated by voltammetric method in this paper. In pH 2.0 Britton-Robinson (B-R) buffer solution orange G displayed an irreversible voltammetric reduction peak at -0.17 V (vs. SCE) on mercury working electrode. The addition of human serum albumin (HSA) into the orange G solution resulted in the decrease of the reduction current peak apparently without the changes of peak potentials and no new peaks appeared. The electrochemical parameters of orange G solution in the absence and presence of HSA were calculated and compared. The results showed that there were no significant changes, which indicated that the electrochemical behaviors of reaction solution on the mercury working electrode showed no changes and a supramolecular electrochemical inactive biocomplex was formed. The interaction mechanism was due to the formation of the microelectrostatic field in albumin structure in aqueous solution and caused the interaction with orange G, which induced the decrease of the equilibrium concentration of orange G in the reaction solution, and the decrease of the reductive peak current. The interaction conditions were discussed carefully. Under the optimal conditions the decrease of peak current was proportional to the concentration of protein and further used to the determination of different kinds of proteins. The calibration curves for the determination of HSA, bovine serum albumin (BSA), ovalbumin (OVA), bovine hemoglobin (BHb), lipase were linear over the ranges of 4.0~28.0 mg L-1, 4.0~30.0 mg L-1, 2.0~20.0 mg L-1, 2.0~25.0 mg L-1, 2.0~30.0 mg L-1, respectively. The detection limit was 3.0 mg L-1 for HSA, 3.5 mg L-1 for BSA, 1.0 mg L-1 for OVA, BHb and lipase. The new established electrochemical method was applied to determine the content of albumin in healthy human serum samples and the results were in good agreement with the traditional Coomassie Brilliant Blue (GBB G-250) spectrophotometric method.
abstract_unstemmed	The interaction of orange G with protein was investigated by voltammetric method in this paper. In pH 2.0 Britton-Robinson (B-R) buffer solution orange G displayed an irreversible voltammetric reduction peak at -0.17 V (vs. SCE) on mercury working electrode. The addition of human serum albumin (HSA) into the orange G solution resulted in the decrease of the reduction current peak apparently without the changes of peak potentials and no new peaks appeared. The electrochemical parameters of orange G solution in the absence and presence of HSA were calculated and compared. The results showed that there were no significant changes, which indicated that the electrochemical behaviors of reaction solution on the mercury working electrode showed no changes and a supramolecular electrochemical inactive biocomplex was formed. The interaction mechanism was due to the formation of the microelectrostatic field in albumin structure in aqueous solution and caused the interaction with orange G, which induced the decrease of the equilibrium concentration of orange G in the reaction solution, and the decrease of the reductive peak current. The interaction conditions were discussed carefully. Under the optimal conditions the decrease of peak current was proportional to the concentration of protein and further used to the determination of different kinds of proteins. The calibration curves for the determination of HSA, bovine serum albumin (BSA), ovalbumin (OVA), bovine hemoglobin (BHb), lipase were linear over the ranges of 4.0~28.0 mg L-1, 4.0~30.0 mg L-1, 2.0~20.0 mg L-1, 2.0~25.0 mg L-1, 2.0~30.0 mg L-1, respectively. The detection limit was 3.0 mg L-1 for HSA, 3.5 mg L-1 for BSA, 1.0 mg L-1 for OVA, BHb and lipase. The new established electrochemical method was applied to determine the content of albumin in healthy human serum samples and the results were in good agreement with the traditional Coomassie Brilliant Blue (GBB G-250) spectrophotometric method.
collection_details	GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700
container_issue	3
title_short	Voltammetric studies on the interaction of orange G with proteins: analytical applications
url	https://doaj.org/article/da500cb5b88b4ff4af27e9d27a17f97d http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532006000300012 https://doaj.org/toc/0103-5053 https://doaj.org/toc/1678-4790
remote_bool	true
author2	Han Junying Ren Yong Jiao Kui
author2Str	Han Junying Ren Yong Jiao Kui
ppnlink	32461330X
callnumber-subject	QD - Chemistry
mediatype_str_mv	c
isOA_txt	true
hochschulschrift_bool	false
callnumber-a	QD1-999
up_date	2024-07-03T17:05:21.555Z
_version_	1803578320151904256
fullrecord_marcxml	<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">DOAJ078292662</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230309155812.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">230228s2006 xx \|\|\|\|\|o 00\| \|\|eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)DOAJ078292662</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)DOAJda500cb5b88b4ff4af27e9d27a17f97d</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="050" ind1=" " ind2="0"><subfield code="a">QD1-999</subfield></datafield><datafield tag="100" ind1="0" ind2=" "><subfield code="a">Sun Wei</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Voltammetric studies on the interaction of orange G with proteins: analytical applications</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2006</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">Computermedien</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">The interaction of orange G with protein was investigated by voltammetric method in this paper. In pH 2.0 Britton-Robinson (B-R) buffer solution orange G displayed an irreversible voltammetric reduction peak at -0.17 V (vs. SCE) on mercury working electrode. The addition of human serum albumin (HSA) into the orange G solution resulted in the decrease of the reduction current peak apparently without the changes of peak potentials and no new peaks appeared. The electrochemical parameters of orange G solution in the absence and presence of HSA were calculated and compared. The results showed that there were no significant changes, which indicated that the electrochemical behaviors of reaction solution on the mercury working electrode showed no changes and a supramolecular electrochemical inactive biocomplex was formed. The interaction mechanism was due to the formation of the microelectrostatic field in albumin structure in aqueous solution and caused the interaction with orange G, which induced the decrease of the equilibrium concentration of orange G in the reaction solution, and the decrease of the reductive peak current. The interaction conditions were discussed carefully. Under the optimal conditions the decrease of peak current was proportional to the concentration of protein and further used to the determination of different kinds of proteins. The calibration curves for the determination of HSA, bovine serum albumin (BSA), ovalbumin (OVA), bovine hemoglobin (BHb), lipase were linear over the ranges of 4.0~28.0 mg L-1, 4.0~30.0 mg L-1, 2.0~20.0 mg L-1, 2.0~25.0 mg L-1, 2.0~30.0 mg L-1, respectively. The detection limit was 3.0 mg L-1 for HSA, 3.5 mg L-1 for BSA, 1.0 mg L-1 for OVA, BHb and lipase. The new established electrochemical method was applied to determine the content of albumin in healthy human serum samples and the results were in good agreement with the traditional Coomassie Brilliant Blue (GBB G-250) spectrophotometric method.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">orange G</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">human serum albumin</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">voltammetry</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">interaction</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">supramolecule</subfield></datafield><datafield tag="653" ind1=" " ind2="0"><subfield code="a">Chemistry</subfield></datafield><datafield tag="700" ind1="0" ind2=" "><subfield code="a">Han Junying</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="0" ind2=" "><subfield code="a">Ren Yong</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="0" ind2=" "><subfield code="a">Jiao Kui</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">In</subfield><subfield code="t">Journal of the Brazilian Chemical Society</subfield><subfield code="d">Sociedade Brasileira de Química, 2017</subfield><subfield code="g">17(2006), 3, Seite 510-517</subfield><subfield code="w">(DE-627)32461330X</subfield><subfield code="w">(DE-600)2028738-0</subfield><subfield code="x">16784790</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:17</subfield><subfield code="g">year:2006</subfield><subfield code="g">number:3</subfield><subfield code="g">pages:510-517</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">https://doaj.org/article/da500cb5b88b4ff4af27e9d27a17f97d</subfield><subfield code="z">kostenfrei</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532006000300012</subfield><subfield code="z">kostenfrei</subfield></datafield><datafield tag="856" ind1="4" ind2="2"><subfield code="u">https://doaj.org/toc/0103-5053</subfield><subfield code="y">Journal toc</subfield><subfield code="z">kostenfrei</subfield></datafield><datafield tag="856" ind1="4" ind2="2"><subfield code="u">https://doaj.org/toc/1678-4790</subfield><subfield code="y">Journal toc</subfield><subfield code="z">kostenfrei</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SYSFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_DOAJ</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_20</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_22</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_23</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_24</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_39</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_40</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_60</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_62</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_63</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_65</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_69</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_70</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_73</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_95</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_105</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_110</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_151</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_161</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_170</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_213</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_230</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_285</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_293</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_602</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2014</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4012</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4037</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4112</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4125</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4126</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4249</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4305</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4306</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4307</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4313</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4322</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4323</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4324</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4325</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4338</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4367</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4700</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">17</subfield><subfield code="j">2006</subfield><subfield code="e">3</subfield><subfield code="h">510-517</subfield></datafield></record></collection>
score	7.3996515

Nicht das Richtige dabei?

Schreiben Sie uns!

Voltammetric studies on the interaction of orange G with proteins: analytical applications

Nicht das Richtige dabei?

Zugang & Verfügbarkeit

Vorhandene Bände

Nicht das Richtige dabei?