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Refolding a disulfide dimer of cytochrome c.

Abstract：

:A covalent dimer of Saccharomyces cerevisiae iso-1 cytochrome c is stabilized by an interchain disulfide bond involving the cysteine residue penultimate to the C-terminus. The individual chains in the dimer appear to retain the tertiary structural features characteristic for monomeric cytochrome c albeit with some perturbation. The dimer is reversibly denatured by heat, urea, or guanidine hydrochloride in a single cooperative transition whose midpoint is less than that of the monomeric protein. The kinetic profile observed for the refolding of the denatured dimer is characteristic for monomeric cytochromes except for a markedly enhanced slow-phase amplitude.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Bryant C,Strottmann JM,Stellwagen E

doi

10.1021/bi00335a011

subject

Has Abstract

pub_date

1985-07-02 00:00:00

pages

3459-64

issue

14

eissn

0006-2960

issn

1520-4995

journal_volume

24

pub_type

杂志文章

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