Nagelschmidt M, Unger T, Struck H
Biochim Biophys Acta. 1979 Nov 9;571(1):105-11. doi: 10.1016/0005-2744(79)90230-4.
A peptidase cleaving a synthetic substrate for collagen peptidases, 4-phenylazobenzyloxcarbonyl-L-Pro-L-Leu-Gly-L-pro-D-Arg (designated as PZ-peptide) has been purified 1200-fold from rabbit serum and characterized. The enzyme preparation is free of collagenase and unspecific proteinase activity. The natural substrates are denatured collagen and collagen peptides. The peptidase has a molecular weight of 124 000 and an isoelectric point at pH 5.1. The pH dependence curve exhibits two maxima, one at pH 7.1 and the other at pH 7.9. The enzymic reaction is completely inhibited by Zn2+ and to a slower degree by Hg2+, Mn2+ and p-hydroxymercuribenzoate. It is not affected by EDTA and KCN but totally blocked by o-phenanthroline. Phenylmethylsulfonylfluoride is completely inhibitory and points to a serine residue in the active site.
一种能切割胶原蛋白肽酶合成底物4-苯偶氮苄氧羰基-L-脯氨酸-L-亮氨酸-Gly-L-脯氨酸-D-精氨酸（命名为PZ-肽）的肽酶已从兔血清中纯化了1200倍并进行了表征。该酶制剂不含胶原酶和非特异性蛋白酶活性。天然底物是变性胶原蛋白和胶原蛋白肽。该肽酶的分子量为124000，等电点为pH 5.1。pH依赖性曲线有两个最大值，一个在pH 7.1，另一个在pH 7.9。酶促反应被Zn2+完全抑制，被Hg2+、Mn2+和对羟基汞苯甲酸抑制的程度较慢。它不受EDTA和KCN影响，但被邻菲罗啉完全阻断。苯甲基磺酰氟具有完全抑制作用，表明活性位点存在丝氨酸残基。
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