The role of the intrachain disulfide bond in the conformation and stability of the constant fragment of the immunoglobulin light chain.

Abstract:

:The conformation and stabilities of the CL fragment isolated from a type lambda Bence Jones protein and the fragment in which the intrachain disulfide bond had been reduced were studied by measuring CD, fluorescence, and ultraviolet absorption. The results indicated that no great conformational change occurs on reduction of the disulfide, unless the SH groups are alkylated. Intact CL was more resistant than reduced CL to guanidine hydrochloride. The denaturation curves were analyzed using an equation based on the binding of guanidine hydrochloride and the free energy changes of denaturation in the absence of the denaturant were estimated as about 6 kcal.mol-1 for intact CL and about 1.8 kcal.mol-1 for reduced CL. The difference in stability between intact CL and reduced CL was explained to a great extent in terms of the entropy change associated with reduction of the intrachain disulfide bond of the fragment in the denatured state.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Goto Y,Hamaguchi K

doi

10.1093/oxfordjournals.jbchem.a132661

keywords:

subject

Has Abstract

pub_date

1979-11-01 00:00:00

pages

1433-41

issue

5

eissn

0021-924X

issn

1756-2651

journal_volume

86

pub_type

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