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. 1984 Nov 15;224(1):227–233. doi: 10.1042/bj2240227

Biosynthesis of a disulphide-bonded short-chain collagen by calf growth-plate cartilage.

M C Remington, R I Bashey, C T Brighton, S A Jimenez
PMCID: PMC1144417  PMID: 6095816

Abstract

Collagen biosynthesis by organ cultures of the hypertrophic zone of calf growth-plate cartilage was studied. It was found that this tissue devotes a large portion of its biosynthetic commitment towards production of a collagen molecule comprising short collagen chains. This collagen is similar to short-chain collagens synthesized by chick-embryo tibiotarsus, rabbit growth-plate cartilage and chick chondrocytes grown in three-dimensional gels. However, in contrast with the collagen synthesized in these three systems, the short-chain collagen synthesized by calf growth-plate hypertrophic cartilage is stabilized by disulphide bonds localized within the pepsin-resistant triple-helical collagenous domains of these molecules.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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