Optical responses of BSA protein under re-entrant condensation in presence of trivalent ions

Fluorescence behavior of globular protein like BSA is studied under the re-entrant condensation in the presence of trivalent salts like YCl3 and LaCl3. BSA shows a re-entrant behaviour in solution where a specific turbid phase is formed between the two critical concentrations of the trivalent salts....
Ausführliche Beschreibung

Gespeichert in:

Autor*in:	Pandit, Subhankar [verfasserIn] Kundu, Sarathi [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2018

Schlagwörter:	Bovine serum albumin Tri-valent ions UV–vis spectroscopy Fluorescence spectroscopy

Übergeordnetes Werk:	Enthalten in: Journal of molecular liquids - New York, NY [u.a.] : Elsevier, 1983, 276, Seite 954-960
Übergeordnetes Werk:	volume:276 ; pages:954-960

DOI / URN:	10.1016/j.molliq.2018.12.122

Katalog-ID:	ELV001651420

Internformat


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520			\|a Fluorescence behavior of globular protein like BSA is studied under the re-entrant condensation in the presence of trivalent salts like YCl3 and LaCl3. BSA shows a re-entrant behaviour in solution where a specific turbid phase is formed between the two critical concentrations of the trivalent salts. Optical behaviors of proteins are explored by UV–Vis, photoluminescence and time resolved photoluminescence (TRPL) spectroscopy, whereas hydrodynamic size is obtained from the dynamic light scattering (DLS) technique. BSA shows maximum emission intensity at ≈338 nm for an excitation at 278 nm, however, the value of the peak intensity of emission gradually increases with the increase in salt concentration and becomes maximum at the turbid phase but for higher salt concentration as the re-dissolution takes place, the emission intensity again decreases. TRPL study suggests that the decay time of BSA under re-entrant condensation is correlated with the salt concentration, whereas DLS study shows that the hydrodynamic size gradually increases up to a certain salt concentration where turbid phase is formed and then again decreases for higher salt concentrations. The variation of emission intensity of BSA nearly follows the modification of diffusion coefficient or hydrodynamic size and the phase transition behaviors.
650		4	\|a Bovine serum albumin
650		4	\|a Tri-valent ions
650		4	\|a UV–vis spectroscopy
650		4	\|a Fluorescence spectroscopy
700	1		\|a Kundu, Sarathi \|e verfasserin \|4 aut
773	0	8	\|i Enthalten in \|t Journal of molecular liquids \|d New York, NY [u.a.] : Elsevier, 1983 \|g 276, Seite 954-960 \|h Online-Ressource \|w (DE-627)302469664 \|w (DE-600)1491496-7 \|w (DE-576)259483915 \|x 1873-3166 \|7 nnns
773	1	8	\|g volume:276 \|g pages:954-960
912			\|a GBV_USEFLAG_U
912			\|a SYSFLAG_U
912			\|a GBV_ELV
912			\|a SSG-OLC-PHA
912			\|a GBV_ILN_20
912			\|a GBV_ILN_22
912			\|a GBV_ILN_23
912			\|a GBV_ILN_24
912			\|a GBV_ILN_31
912			\|a GBV_ILN_32
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_74
912			\|a GBV_ILN_90
912			\|a GBV_ILN_95
912			\|a GBV_ILN_100
912			\|a GBV_ILN_101
912			\|a GBV_ILN_105
912			\|a GBV_ILN_110
912			\|a GBV_ILN_150
912			\|a GBV_ILN_151
912			\|a GBV_ILN_224
912			\|a GBV_ILN_370
912			\|a GBV_ILN_374
912			\|a GBV_ILN_602
912			\|a GBV_ILN_702
912			\|a GBV_ILN_2003
912			\|a GBV_ILN_2004
912			\|a GBV_ILN_2005
912			\|a GBV_ILN_2011
912			\|a GBV_ILN_2014
912			\|a GBV_ILN_2015
912			\|a GBV_ILN_2020
912			\|a GBV_ILN_2021
912			\|a GBV_ILN_2025
912			\|a GBV_ILN_2027
912			\|a GBV_ILN_2034
912			\|a GBV_ILN_2038
912			\|a GBV_ILN_2044
912			\|a GBV_ILN_2048
912			\|a GBV_ILN_2049
912			\|a GBV_ILN_2050
912			\|a GBV_ILN_2056
912			\|a GBV_ILN_2059
912			\|a GBV_ILN_2061
912			\|a GBV_ILN_2064
912			\|a GBV_ILN_2065
912			\|a GBV_ILN_2068
912			\|a GBV_ILN_2111
912			\|a GBV_ILN_2112
912			\|a GBV_ILN_2113
912			\|a GBV_ILN_2118
912			\|a GBV_ILN_2122
912			\|a GBV_ILN_2129
912			\|a GBV_ILN_2143
912			\|a GBV_ILN_2147
912			\|a GBV_ILN_2148
912			\|a GBV_ILN_2152
912			\|a GBV_ILN_2153
912			\|a GBV_ILN_2190
912			\|a GBV_ILN_2336
912			\|a GBV_ILN_2507
912			\|a GBV_ILN_2522
912			\|a GBV_ILN_2807
912			\|a GBV_ILN_4035
912			\|a GBV_ILN_4037
912			\|a GBV_ILN_4112
912			\|a GBV_ILN_4125
912			\|a GBV_ILN_4126
912			\|a GBV_ILN_4242
912			\|a GBV_ILN_4251
912			\|a GBV_ILN_4305
912			\|a GBV_ILN_4313
912			\|a GBV_ILN_4323
912			\|a GBV_ILN_4324
912			\|a GBV_ILN_4326
912			\|a GBV_ILN_4333
912			\|a GBV_ILN_4334
912			\|a GBV_ILN_4335
912			\|a GBV_ILN_4338
912			\|a GBV_ILN_4393
936	b	k	\|a 35.21 \|j Lösungen \|j Flüssigkeiten \|x Physikalische Chemie
951			\|a AR
952			\|d 276 \|h 954-960

Indexfelder

author_variant	s p sp s k sk
matchkey_str	article:18733166:2018----::piarsossfspoenneretatodnainn
hierarchy_sort_str	2018
bklnumber	35.21
publishDate	2018
allfields	10.1016/j.molliq.2018.12.122 doi (DE-627)ELV001651420 (ELSEVIER)S0167-7322(18)35089-X DE-627 ger DE-627 rda eng 540 DE-600 35.21 bkl Pandit, Subhankar verfasserin aut Optical responses of BSA protein under re-entrant condensation in presence of trivalent ions 2018 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Fluorescence behavior of globular protein like BSA is studied under the re-entrant condensation in the presence of trivalent salts like YCl3 and LaCl3. BSA shows a re-entrant behaviour in solution where a specific turbid phase is formed between the two critical concentrations of the trivalent salts. Optical behaviors of proteins are explored by UV–Vis, photoluminescence and time resolved photoluminescence (TRPL) spectroscopy, whereas hydrodynamic size is obtained from the dynamic light scattering (DLS) technique. BSA shows maximum emission intensity at ≈338 nm for an excitation at 278 nm, however, the value of the peak intensity of emission gradually increases with the increase in salt concentration and becomes maximum at the turbid phase but for higher salt concentration as the re-dissolution takes place, the emission intensity again decreases. TRPL study suggests that the decay time of BSA under re-entrant condensation is correlated with the salt concentration, whereas DLS study shows that the hydrodynamic size gradually increases up to a certain salt concentration where turbid phase is formed and then again decreases for higher salt concentrations. The variation of emission intensity of BSA nearly follows the modification of diffusion coefficient or hydrodynamic size and the phase transition behaviors. Bovine serum albumin Tri-valent ions UV–vis spectroscopy Fluorescence spectroscopy Kundu, Sarathi verfasserin aut Enthalten in Journal of molecular liquids New York, NY [u.a.] : Elsevier, 1983 276, Seite 954-960 Online-Ressource (DE-627)302469664 (DE-600)1491496-7 (DE-576)259483915 1873-3166 nnns volume:276 pages:954-960 GBV_USEFLAG_U SYSFLAG_U GBV_ELV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 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_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_374 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2807 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 35.21 Lösungen Flüssigkeiten Physikalische Chemie AR 276 954-960
spelling	10.1016/j.molliq.2018.12.122 doi (DE-627)ELV001651420 (ELSEVIER)S0167-7322(18)35089-X DE-627 ger DE-627 rda eng 540 DE-600 35.21 bkl Pandit, Subhankar verfasserin aut Optical responses of BSA protein under re-entrant condensation in presence of trivalent ions 2018 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Fluorescence behavior of globular protein like BSA is studied under the re-entrant condensation in the presence of trivalent salts like YCl3 and LaCl3. BSA shows a re-entrant behaviour in solution where a specific turbid phase is formed between the two critical concentrations of the trivalent salts. Optical behaviors of proteins are explored by UV–Vis, photoluminescence and time resolved photoluminescence (TRPL) spectroscopy, whereas hydrodynamic size is obtained from the dynamic light scattering (DLS) technique. BSA shows maximum emission intensity at ≈338 nm for an excitation at 278 nm, however, the value of the peak intensity of emission gradually increases with the increase in salt concentration and becomes maximum at the turbid phase but for higher salt concentration as the re-dissolution takes place, the emission intensity again decreases. TRPL study suggests that the decay time of BSA under re-entrant condensation is correlated with the salt concentration, whereas DLS study shows that the hydrodynamic size gradually increases up to a certain salt concentration where turbid phase is formed and then again decreases for higher salt concentrations. The variation of emission intensity of BSA nearly follows the modification of diffusion coefficient or hydrodynamic size and the phase transition behaviors. Bovine serum albumin Tri-valent ions UV–vis spectroscopy Fluorescence spectroscopy Kundu, Sarathi verfasserin aut Enthalten in Journal of molecular liquids New York, NY [u.a.] : Elsevier, 1983 276, Seite 954-960 Online-Ressource (DE-627)302469664 (DE-600)1491496-7 (DE-576)259483915 1873-3166 nnns volume:276 pages:954-960 GBV_USEFLAG_U SYSFLAG_U GBV_ELV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 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_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_374 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2807 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 35.21 Lösungen Flüssigkeiten Physikalische Chemie AR 276 954-960
allfields_unstemmed	10.1016/j.molliq.2018.12.122 doi (DE-627)ELV001651420 (ELSEVIER)S0167-7322(18)35089-X DE-627 ger DE-627 rda eng 540 DE-600 35.21 bkl Pandit, Subhankar verfasserin aut Optical responses of BSA protein under re-entrant condensation in presence of trivalent ions 2018 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Fluorescence behavior of globular protein like BSA is studied under the re-entrant condensation in the presence of trivalent salts like YCl3 and LaCl3. BSA shows a re-entrant behaviour in solution where a specific turbid phase is formed between the two critical concentrations of the trivalent salts. Optical behaviors of proteins are explored by UV–Vis, photoluminescence and time resolved photoluminescence (TRPL) spectroscopy, whereas hydrodynamic size is obtained from the dynamic light scattering (DLS) technique. BSA shows maximum emission intensity at ≈338 nm for an excitation at 278 nm, however, the value of the peak intensity of emission gradually increases with the increase in salt concentration and becomes maximum at the turbid phase but for higher salt concentration as the re-dissolution takes place, the emission intensity again decreases. TRPL study suggests that the decay time of BSA under re-entrant condensation is correlated with the salt concentration, whereas DLS study shows that the hydrodynamic size gradually increases up to a certain salt concentration where turbid phase is formed and then again decreases for higher salt concentrations. The variation of emission intensity of BSA nearly follows the modification of diffusion coefficient or hydrodynamic size and the phase transition behaviors. Bovine serum albumin Tri-valent ions UV–vis spectroscopy Fluorescence spectroscopy Kundu, Sarathi verfasserin aut Enthalten in Journal of molecular liquids New York, NY [u.a.] : Elsevier, 1983 276, Seite 954-960 Online-Ressource (DE-627)302469664 (DE-600)1491496-7 (DE-576)259483915 1873-3166 nnns volume:276 pages:954-960 GBV_USEFLAG_U SYSFLAG_U GBV_ELV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 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_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_374 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2807 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 35.21 Lösungen Flüssigkeiten Physikalische Chemie AR 276 954-960
allfieldsGer	10.1016/j.molliq.2018.12.122 doi (DE-627)ELV001651420 (ELSEVIER)S0167-7322(18)35089-X DE-627 ger DE-627 rda eng 540 DE-600 35.21 bkl Pandit, Subhankar verfasserin aut Optical responses of BSA protein under re-entrant condensation in presence of trivalent ions 2018 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Fluorescence behavior of globular protein like BSA is studied under the re-entrant condensation in the presence of trivalent salts like YCl3 and LaCl3. BSA shows a re-entrant behaviour in solution where a specific turbid phase is formed between the two critical concentrations of the trivalent salts. Optical behaviors of proteins are explored by UV–Vis, photoluminescence and time resolved photoluminescence (TRPL) spectroscopy, whereas hydrodynamic size is obtained from the dynamic light scattering (DLS) technique. BSA shows maximum emission intensity at ≈338 nm for an excitation at 278 nm, however, the value of the peak intensity of emission gradually increases with the increase in salt concentration and becomes maximum at the turbid phase but for higher salt concentration as the re-dissolution takes place, the emission intensity again decreases. TRPL study suggests that the decay time of BSA under re-entrant condensation is correlated with the salt concentration, whereas DLS study shows that the hydrodynamic size gradually increases up to a certain salt concentration where turbid phase is formed and then again decreases for higher salt concentrations. The variation of emission intensity of BSA nearly follows the modification of diffusion coefficient or hydrodynamic size and the phase transition behaviors. Bovine serum albumin Tri-valent ions UV–vis spectroscopy Fluorescence spectroscopy Kundu, Sarathi verfasserin aut Enthalten in Journal of molecular liquids New York, NY [u.a.] : Elsevier, 1983 276, Seite 954-960 Online-Ressource (DE-627)302469664 (DE-600)1491496-7 (DE-576)259483915 1873-3166 nnns volume:276 pages:954-960 GBV_USEFLAG_U SYSFLAG_U GBV_ELV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 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_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_374 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2807 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 35.21 Lösungen Flüssigkeiten Physikalische Chemie AR 276 954-960
allfieldsSound	10.1016/j.molliq.2018.12.122 doi (DE-627)ELV001651420 (ELSEVIER)S0167-7322(18)35089-X DE-627 ger DE-627 rda eng 540 DE-600 35.21 bkl Pandit, Subhankar verfasserin aut Optical responses of BSA protein under re-entrant condensation in presence of trivalent ions 2018 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Fluorescence behavior of globular protein like BSA is studied under the re-entrant condensation in the presence of trivalent salts like YCl3 and LaCl3. BSA shows a re-entrant behaviour in solution where a specific turbid phase is formed between the two critical concentrations of the trivalent salts. Optical behaviors of proteins are explored by UV–Vis, photoluminescence and time resolved photoluminescence (TRPL) spectroscopy, whereas hydrodynamic size is obtained from the dynamic light scattering (DLS) technique. BSA shows maximum emission intensity at ≈338 nm for an excitation at 278 nm, however, the value of the peak intensity of emission gradually increases with the increase in salt concentration and becomes maximum at the turbid phase but for higher salt concentration as the re-dissolution takes place, the emission intensity again decreases. TRPL study suggests that the decay time of BSA under re-entrant condensation is correlated with the salt concentration, whereas DLS study shows that the hydrodynamic size gradually increases up to a certain salt concentration where turbid phase is formed and then again decreases for higher salt concentrations. The variation of emission intensity of BSA nearly follows the modification of diffusion coefficient or hydrodynamic size and the phase transition behaviors. Bovine serum albumin Tri-valent ions UV–vis spectroscopy Fluorescence spectroscopy Kundu, Sarathi verfasserin aut Enthalten in Journal of molecular liquids New York, NY [u.a.] : Elsevier, 1983 276, Seite 954-960 Online-Ressource (DE-627)302469664 (DE-600)1491496-7 (DE-576)259483915 1873-3166 nnns volume:276 pages:954-960 GBV_USEFLAG_U SYSFLAG_U GBV_ELV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 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_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_374 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2807 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 35.21 Lösungen Flüssigkeiten Physikalische Chemie AR 276 954-960
language	English
source	Enthalten in Journal of molecular liquids 276, Seite 954-960 volume:276 pages:954-960
sourceStr	Enthalten in Journal of molecular liquids 276, Seite 954-960 volume:276 pages:954-960
format_phy_str_mv	Article
bklname	Lösungen Flüssigkeiten
institution	findex.gbv.de
topic_facet	Bovine serum albumin Tri-valent ions UV–vis spectroscopy Fluorescence spectroscopy
dewey-raw	540
isfreeaccess_bool	false
container_title	Journal of molecular liquids
authorswithroles_txt_mv	Pandit, Subhankar @@aut@@ Kundu, Sarathi @@aut@@
publishDateDaySort_date	2018-01-01T00:00:00Z
hierarchy_top_id	302469664
dewey-sort	3540
id	ELV001651420
language_de	englisch
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author	Pandit, Subhankar
spellingShingle	Pandit, Subhankar ddc 540 bkl 35.21 misc Bovine serum albumin misc Tri-valent ions misc UV–vis spectroscopy misc Fluorescence spectroscopy Optical responses of BSA protein under re-entrant condensation in presence of trivalent ions
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topic_title	540 DE-600 35.21 bkl Optical responses of BSA protein under re-entrant condensation in presence of trivalent ions Bovine serum albumin Tri-valent ions UV–vis spectroscopy Fluorescence spectroscopy
topic	ddc 540 bkl 35.21 misc Bovine serum albumin misc Tri-valent ions misc UV–vis spectroscopy misc Fluorescence spectroscopy
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title	Optical responses of BSA protein under re-entrant condensation in presence of trivalent ions
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title_full	Optical responses of BSA protein under re-entrant condensation in presence of trivalent ions
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title_sort	optical responses of bsa protein under re-entrant condensation in presence of trivalent ions
title_auth	Optical responses of BSA protein under re-entrant condensation in presence of trivalent ions
abstract	Fluorescence behavior of globular protein like BSA is studied under the re-entrant condensation in the presence of trivalent salts like YCl3 and LaCl3. BSA shows a re-entrant behaviour in solution where a specific turbid phase is formed between the two critical concentrations of the trivalent salts. Optical behaviors of proteins are explored by UV–Vis, photoluminescence and time resolved photoluminescence (TRPL) spectroscopy, whereas hydrodynamic size is obtained from the dynamic light scattering (DLS) technique. BSA shows maximum emission intensity at ≈338 nm for an excitation at 278 nm, however, the value of the peak intensity of emission gradually increases with the increase in salt concentration and becomes maximum at the turbid phase but for higher salt concentration as the re-dissolution takes place, the emission intensity again decreases. TRPL study suggests that the decay time of BSA under re-entrant condensation is correlated with the salt concentration, whereas DLS study shows that the hydrodynamic size gradually increases up to a certain salt concentration where turbid phase is formed and then again decreases for higher salt concentrations. The variation of emission intensity of BSA nearly follows the modification of diffusion coefficient or hydrodynamic size and the phase transition behaviors.
abstractGer	Fluorescence behavior of globular protein like BSA is studied under the re-entrant condensation in the presence of trivalent salts like YCl3 and LaCl3. BSA shows a re-entrant behaviour in solution where a specific turbid phase is formed between the two critical concentrations of the trivalent salts. Optical behaviors of proteins are explored by UV–Vis, photoluminescence and time resolved photoluminescence (TRPL) spectroscopy, whereas hydrodynamic size is obtained from the dynamic light scattering (DLS) technique. BSA shows maximum emission intensity at ≈338 nm for an excitation at 278 nm, however, the value of the peak intensity of emission gradually increases with the increase in salt concentration and becomes maximum at the turbid phase but for higher salt concentration as the re-dissolution takes place, the emission intensity again decreases. TRPL study suggests that the decay time of BSA under re-entrant condensation is correlated with the salt concentration, whereas DLS study shows that the hydrodynamic size gradually increases up to a certain salt concentration where turbid phase is formed and then again decreases for higher salt concentrations. The variation of emission intensity of BSA nearly follows the modification of diffusion coefficient or hydrodynamic size and the phase transition behaviors.
abstract_unstemmed	Fluorescence behavior of globular protein like BSA is studied under the re-entrant condensation in the presence of trivalent salts like YCl3 and LaCl3. BSA shows a re-entrant behaviour in solution where a specific turbid phase is formed between the two critical concentrations of the trivalent salts. Optical behaviors of proteins are explored by UV–Vis, photoluminescence and time resolved photoluminescence (TRPL) spectroscopy, whereas hydrodynamic size is obtained from the dynamic light scattering (DLS) technique. BSA shows maximum emission intensity at ≈338 nm for an excitation at 278 nm, however, the value of the peak intensity of emission gradually increases with the increase in salt concentration and becomes maximum at the turbid phase but for higher salt concentration as the re-dissolution takes place, the emission intensity again decreases. TRPL study suggests that the decay time of BSA under re-entrant condensation is correlated with the salt concentration, whereas DLS study shows that the hydrodynamic size gradually increases up to a certain salt concentration where turbid phase is formed and then again decreases for higher salt concentrations. The variation of emission intensity of BSA nearly follows the modification of diffusion coefficient or hydrodynamic size and the phase transition behaviors.
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title_short	Optical responses of BSA protein under re-entrant condensation in presence of trivalent ions
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doi_str	10.1016/j.molliq.2018.12.122
up_date	2024-07-06T22:06:27.154Z
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Optical responses of BSA protein under re-entrant condensation in presence of trivalent ions

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