Article
A type I collagen with substitution of a cysteine for glycine-748 in the alpha 1(I) chain copolymerizes with normal type I collagen and can generate fractallike structures.
Biochemistry - 21 May 1991
Kadler K E, Torre-Blanco A, Adachi E, Vogel B E, Hojima Y, Prockop D J
Abstract excerpt
Type I procollagen was purified from cultured fibroblasts of a proband with a lethal variant of osteogenesis imperfecta. The protein was a mixture of normal procollagen and mutated procollagens containing a substitution of cysteine for glycine in either one pro alpha 1(I) chain or both pro alpha...
Topics
- Cells, Cultured
- Collagen
- Cysteine
- Electrophoresis, Polyacrylamide Gel
- Fibroblasts
- Glycine
- Humans
- Kinetics
- Macromolecular Substances
- Models, Structural
- Mutation
- Osteogenesis Imperfecta
- Procollagen
- Protein Conformation
- Reference Values
- Skin