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Article

Mutations in the B-domain of insulin-like growth factor-I influence the oxidative folding to yield products with modified biological properties.

The Biochemical journal - 15 Jun 1995

Milner S J, Francis G L, Wallace J C, Magee B A, Ballard F J

Abstract excerpt

The oxidative folding of human insulin-like growth factor (IGF)-I yields two major disulphide folding isomers. In the present study, B-domain analogues of IGF-I were used to investigate the effect of mutations on the folding reaction and to investigate the functional implications of misfolding. The analogues used were substitutions of the native Glu3 by Gly or Arg, or the native Glu9 by Lys. IGF-I and these...

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Identifiers

PMID: 8948444
DOI: 10.1042/bj3080865
PMCID: PMC1136804

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