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Disulfide isoforms of recombinant glia maturation factor beta.

Abstract：

:Recombinant human glia maturation factor beta (r-hGMF-beta) is a single-chain polypeptide (141 amino acid residues) containing three cysteines, at positions 7, 86 and 95. Nascent r-hGMF-beta exists in the reduced state and has no biological activity. The protein can be activated through oxidative refolding by incubation with a mixture of reduced and oxidized glutathione. Reverse-phase HPLC analysis of the refolded r-hGMF-beta shows the presence of four peaks, corresponding to the reduced form plus three newly generated intrachain disulfide-containing isoforms predicted from the number of cysteine residues. Only one isoform shows biological activity when tested for growth suppression on C6 glioma cells. We infer from the HPLC elution pattern that the active form contains the disulfide bridge Cys86-Cys95.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Zaheer A,Lim R

doi

10.1016/0006-291x(90)91209-b

subject

Has Abstract

pub_date

1990-09-14 00:00:00

pages

746-51

issue

2

eissn

0006-291X

issn

1090-2104

pii

0006-291X(90)91209-B

journal_volume

171

pub_type

杂志文章

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