期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1974
卷号：71
期号：1
页码：40-44
DOI：10.1073/pnas.71.1.40
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：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 [α]1 and [α]2, to [α]1 and [α]2, 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.
