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. 1974 Jan;71(1):40–44. doi: 10.1073/pnas.71.1.40

Calf Tendon Procollagen Peptidase: Its Purification and Endopeptidase Mode of Action

Leonard D Kohn *, Chaviva Isersky *, James Zupnik †, Albert Lenaers †, George Lee *,‡, Charles M Lapière †
PMCID: PMC387927  PMID: 4204204

Abstract

The procollagen peptidase activity of calf tendon has been purified. The enzyme has a high degree of specificity for native procollagen and converts both pro α1 and α2, to α1 and α2, respectively. The purified enzyme is an endopeptidase which excises the amino terminal peptide extensions of the precursor chains in block; the molecular size and amino-acid composition of the excised peptides compare favorably with those predicted in previous reports. Antisera to the enzyme and to procollagen have been prepared and have been used to characterize the enzyme, the enzymatically excised peptides, and the enzyme-peptide complex in reaction mixtures.

Keywords: dermatosparaxis, antiprocollagen peptidase, antiprocollagen

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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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