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. 1972 Nov;69(11):3260–3262. doi: 10.1073/pnas.69.11.3260

Production of Procollagen by Human Fibroblasts in Culture

Barbara D Smith 1, Peter H Byers 1, George R Martin 1
PMCID: PMC389749  PMID: 4508318

Abstract

Three hydroxyproline-containing proteins secreted into the medium by human fibroblasts in culture were isolated and characterized. A minor fraction was identical to the collagen monomer. The major fraction was a form of procollagen, which contained, in addition to pro α and α chains, a component estimated to have a molecular weight of 250,000. This component was a dimer of pro α chains joined by disulfide bonds. The third fraction, much lower in hydroxyproline and hydroxylysine content, was of still greater size. Pro α chains were released upon denaturation and reduction, indicating that this fraction may contain pro α chains linked by disulfide bonds to noncollagenous material.

Keywords: collagen synthesis, connective tissue, chromatography, disulfide linkage

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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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