Aswanikumar S, Radhakrishnan A N
Biochim Biophys Acta. 1975 Mar 28;384(1):194-202. doi: 10.1016/0005-2744(75)90108-4.
A peptidase cleaving a synthetic substrate for collagenase, 4-phenylazobenzyloxycarbonyl-L-Pro-L-Leu-Gly-L-Pro-D-Arg (designated as PZ-peptide) has been purified extensively (about 5200-fold) from a soluble extract of monkey kidney with a view of carrying out studies on its possible physiological role. The purified PZ-peptidase appeared essentially free of collagenase, nonspecific protease and di- and tri-peptidase activities. The properties of the purified PZ-peptidase resemble very much the granuloma enzyme. It is optimally active around pH 7.0. Its apparent Km value for PZ-peptide is 0.72 mM and V is 10.1 mumol/mg protein/min. It is reversibly inhibited by p-hydroxymercuribenzoate and HgCl2, whereas iodoactetamide does not affect the enzyme activity. N-Ethylmaleimide inhibited the enzyme partially (50%). Heavy metals like Cu-2+, Cd-2+, Ag+, Pb-2+, Ni-2+, and Zn-2+ completely inhibited the enzyme activity, while the inhibition by Co-2+ was only partial. Fe-2+ did not exert any effect on the activity. The enzyme activity was completely inhibited by EDTA and was restored almost to the original value by metal ions like Mn-2+, Mg-2+, Ca-2+ and Ba-2+. The approximate molecular weight of the purified enzyme was estimated to be 56 000.
一种能切割胶原酶合成底物4-苯基偶氮苄氧羰基-L-脯氨酸-L-亮氨酸-甘氨酸-L-脯氨酸-D-精氨酸（命名为PZ-肽）的肽酶已从猴肾的可溶性提取物中得到广泛纯化（约5200倍），目的是研究其可能的生理作用。纯化后的PZ-肽酶基本不含胶原酶、非特异性蛋白酶以及二肽酶和三肽酶活性。纯化后的PZ-肽酶的特性与肉芽肿酶非常相似。它在pH 7.0左右活性最佳。其对PZ-肽的表观Km值为0.72 mM，V为10.1 μmol/mg蛋白质/分钟。它可被对羟基汞苯甲酸酯和HgCl2可逆抑制，而碘乙酰胺不影响酶活性。N-乙基马来酰胺部分抑制该酶（50%）。Cu2+、Cd2+、Ag+、Pb2+、Ni2+和Zn2+等重金属完全抑制酶活性，而Co2+的抑制作用只是部分的。Fe2+对活性没有任何影响。该酶的活性被EDTA完全抑制，而Mn2+、Mg2+、Ca2+和Ba2+等金属离子可使其活性几乎恢复到原始值。纯化酶的近似分子量估计为56000。
