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)...
Ausführliche Beschreibung
Autor*in: |
Sun Wei [verfasserIn] Han Junying [verfasserIn] Ren Yong [verfasserIn] Jiao Kui [verfasserIn] |
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E-Artikel |
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Englisch |
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2006 |
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Übergeordnetes Werk: |
In: Journal of the Brazilian Chemical Society - Sociedade Brasileira de Química, 2017, 17(2006), 3, Seite 510-517 |
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Übergeordnetes Werk: |
volume:17 ; year:2006 ; number:3 ; pages:510-517 |
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Katalog-ID: |
DOAJ078292662 |
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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. | ||
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(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 |
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(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 |
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(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 |
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(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 |
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(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 |
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<?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. 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voltammetric studies on the interaction of orange g with proteins: analytical applications |
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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. |
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Voltammetric studies on the interaction of orange G with proteins: analytical applications |
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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. 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