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Titolo:
Interaction of bovine serum albumin with anionic surfactants
Autore:
Deep, S; Ahluwalia, JC;
Indirizzi:
Indian Inst Technol, Dept Chem, New Delhi 110016, India Indian Inst Technol New Delhi India 110016 Chem, New Delhi 110016, India
Titolo Testata:
PHYSICAL CHEMISTRY CHEMICAL PHYSICS
fascicolo: 20, volume: 3, anno: 2001,
pagine: 4583 - 4591
SICI:
1463-9076(2001)3:20<4583:IOBSAW>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
DIFFERENTIAL SCANNING CALORIMETRY; NORMAL-DODECYL SULFATE; THERMAL-DENATURATION; ASPARTATE TRANSCARBAMOYLASE; ESCHERICHIA-COLI; IONIC-STRENGTH; PROTEINS; WATER; UREA; DISSOCIATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
43
Recensione:
Indirizzi per estratti:
Indirizzo: Ahluwalia, JC Indian Inst Technol, Dept Chem, Hauz Khas, New Delhi 110016,India Indian Inst Technol Hauz Khas New Delhi India 110016 India
Citazione:
S. Deep e J.C. Ahluwalia, "Interaction of bovine serum albumin with anionic surfactants", PHYS CHEM P, 3(20), 2001, pp. 4583-4591

Abstract

The effect of binding and conformational changes induced by anionic surfactants sodium dodecyl sulfate (SDS) and sodium octyl sulfate (SOS) on bovineserum albumin (BSA) have been studied using differential scanning calorimetry (DSC), circular dichroism (CD), fluorescence and UV spectroscopic methods. The denaturation temperature, van't Hoff enthalpy and calorimetric enthalpy of BSA in the presence of SDS and SOS and urea at pH 7 have been determined. The results indicate that SDS plays two opposite roles in the folding and stability of BSA. It acts as a structure stabiliser at a low molar concentration ratio of SDS/BSA and as a destabilizer at a higher concentration ratio as a result of binding of SDS to denatured BSA. The Brandts and Linmodel has been used to simulate the results.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 31/03/20 alle ore 10:04:39