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Titolo:
PROTEIN STABILITY FUNCTION RELATIONS - BETA-LACTOGLOBULIN-A SULFHYDRYL-GROUP REACTIVITY AND ITS RELATIONSHIP TO PROTEIN UNFOLDING STABILITY
Autore:
APENTEN RKO;
Indirizzi:
UNIV LEEDS,SCH PHYS SCI,PROCTER DEPT FOOD SCI,WOODHOUSE LANE LEEDS LS2 9JT W YORKSHIRE ENGLAND
Titolo Testata:
International journal of biological macromolecules
fascicolo: 1, volume: 23, anno: 1998,
pagine: 19 - 25
SICI:
0141-8130(1998)23:1<19:PSFR-B>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
MOLTEN GLOBULE STATE; PANCREATIC TRYPSIN-INHIBITOR; BOVINE ALPHA-LACTALBUMIN; HYDROGEN-EXCHANGE; CONFORMATIONAL STABILITIES; THERMAL-DENATURATION; FLEXIBILITY; SURFACE; PH; INTERMEDIATE;
Keywords:
BETA-LACTOGLOBULIN; UREA UNFOLDING; UNFOLDING STABILITY; PROTEIN STABILITY-FUNCTION RELATIONS; SULFHYDRYL GROUP;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
46
Recensione:
Indirizzi per estratti:
Citazione:
R.K.O. Apenten, "PROTEIN STABILITY FUNCTION RELATIONS - BETA-LACTOGLOBULIN-A SULFHYDRYL-GROUP REACTIVITY AND ITS RELATIONSHIP TO PROTEIN UNFOLDING STABILITY", International journal of biological macromolecules, 23(1), 1998, pp. 19-25

Abstract

The effect of protein stability on the reactivity of the free sulphydryl (SH) group in beta-lactoglobulin-A (beta-LgA) provides a model forthe study of protein stability-function relations (PSFR). The free energy change for protein unfolding (Delta G(O)) and SH group exposure (Delta G(SH)) were determined from (i) the urea unfolding curve for beta-LgA and (ii) the kinetics of beta-LgA SH/disulphide exchange with 2-pyridine disulphide (2-PDS) in 0-8 M urea (pH 3). Protein unfolding profiles determined from extrinsic fluorescence and SH-group reactivity measurements were not coincident. beta-LgA formed a stable intermediate (X) state in the presence of 4 M urea with Delta G(O) = 20 (+/- 0.03) kJ/mol. From the low rate of SH/disulphide exchange in 4 M urea, theSH-group within beta-LgA was efficiently masked within the X-state. SH reactivity increased after beta-LgA was unfolded in 6-8 M urea with,Delta G(SH) = 43( +/- 6.4) kJ/mol. Such results are discussed in terms of possible interrelationships between protein unfolding stability and SH reactivity in beta-LgA. (C) 1998 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 10/07/20 alle ore 09:43:03