Dumas J, Hurion N, Weill R, Keil B
FEBS Lett. 1985 Jul 22;187(1):51-5. doi: 10.1016/0014-5793(85)81212-6.
A collagenase cleaving native type I [14C]collagen but inactive against the synthetic substrate Pz-Pro-Leu-Gly-Pro-D-Arg was extracted from mineralized human dental tissue. The enzyme specifically degrades native collagen into characteristic products (3/4) and (1/4). Its apparent molecular mass of 68 kDa is relatively high in comparison with collagenases from other oral tissues. The enzyme is a metalloproteinase inhibited by low concentrations of the chelating agents EDTA, 1, 10-phenanthroline, alpha alpha'-dipyridyl, and not affected by diisopropylfluorophosphate, soybean trypsin inhibitor, and p-chloromercuribenzoate. It is stable to lyophilization and can be stored at-20 degrees C for at least 6 months.
从矿化的人类牙齿组织中提取出一种胶原酶，它能切割天然I型[14C]胶原蛋白，但对合成底物Pz-Pro-Leu-Gly-Pro-D-Arg无活性。该酶能将天然胶原蛋白特异性降解为特征性产物(3/4)和(1/4)。与来自其他口腔组织的胶原酶相比，其表观分子量为68 kDa，相对较高。该酶是一种金属蛋白酶，受低浓度螯合剂乙二胺四乙酸（EDTA）、1,10-菲咯啉、α,α'-联吡啶抑制，不受二异丙基氟磷酸酯、大豆胰蛋白酶抑制剂和对氯汞苯甲酸影响。它对冻干稳定，可在-20℃下储存至少6个月。
