Partial purification of a procollagen C-proteinase. Inhibition by synthetic peptides and sequential cleavage of type I procollagen

摘要: A procollagen C-proteinase which cleaves the C-propeptides from type I was purified about 125-fold membranous bones of chick embryos. As estimated by gel filtration, enzyme 80 000 daltons. When a reaction with modified carried out, preferentially cleaved pro alpha chains in order 1, and then 2. The inhibited several metal chelators high concentrations dithiothreitol. It also 5% fetal calf serum. series inhibitors serine proteinases sulfhydryl-containing were not inhibitory. Four oligopeptides synthesized amino acid sequences similar to around sites at are during conversion top collagen vivo. peptide Tyr-Tyr-Arg-Ala-Asp-Asp-Ala 35--60% 6--12 mM. Shorter peptides containing Ala-Asp bond less effective. partially found cleave II III procollagens.