固定于ARM-琼脂糖上的人血清激肽释放酶的制备及某些性质
Preparation and some properties of human serum kallikrein immobilized on ARM-Sepharose.
作者信息
Kawalec M, Kawiak J, Yarovaya G A, Dotsenko V L, Orekhovich V N
出版信息
Clin Chim Acta. 1979 May 2;93(3):329-33. doi: 10.1016/0009-8981(79)90282-1.
PMID:36246
Abstract
A highly purified human serum kallikrein immobilized on CH-Sepharose 4-B was obtained. KM values for N-benzoyl-L-arginine ethyl ester and N-tosyl-L-arginine methyl ester hydrolysis of this preparation were 1.10 x 10(-3) M and 3.6 x 10(-4) M, respectively; pH optimum of hydrolysis of these esters were found to be 8.2 and 8.5, respectively. The immobilized kallikrein possessed kininogenase activity and was capable of activating prekallikrein.
摘要
获得了一种固定在CH-琼脂糖4-B上的高度纯化的人血清激肽释放酶。该制剂对N-苯甲酰-L-精氨酸乙酯和N-甲苯磺酰-L-精氨酸甲酯水解的米氏常数分别为1.10×10⁻³M和3.6×10⁻⁴M；发现这些酯水解的最适pH分别为8.2和8.5。固定化激肽释放酶具有激肽原酶活性，能够激活前激肽释放酶。
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