Copolymerization of normal type I collagen with three mutated type I collagens containing substitutions of cysteine at different glycine positions in the alpha 1 (I) chain.

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Article

Copolymerization of normal type I collagen with three mutated type I collagens containing substitutions of cysteine at different glycine positions in the alpha 1 (I) chain.

The Journal of biological chemistry - 5 Mar 1992

Torre-Blanco A, Adachi E, Romanic A M, Prockop D J

Abstract excerpt

Previous observations with type I collagen from a proband with lethal osteogenesis imperfecta demonstrated that type I collagen containing a substitution of cysteine for glycine alpha 1-748 copolymerized with normal type I collagen (Kadler, K. E., Torre-Blanco, A., Adachi, E., Vogel, B. E., Hojim...

Topics

Adult
Collagen
Cysteine
Electrophoresis, Polyacrylamide Gel
Fibroblasts
Glycine
Humans
Kinetics
Male
Mutation
Osteogenesis Imperfecta
Procollagen
Skin

Source

Open in PubMed

Identifiers

PMID: 1537873

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-1537873-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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