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. T...
Topics
- Amino Acid Sequence
- Animals
- Cells, Cultured
- Chromatography, High Pressure Liquid
- Disulfides
- Humans
- Insulin-Like Growth Factor I
- Kinetics
- Molecular Sequence Data
- Mutation
- Oxidation-Reduction
- Peptides
- Protein Biosynthesis
- Protein Conformation
- Protein Folding
- Proteins
- Rats
- Receptor, IGF Type 1