Sokolova I A, Khodarev N N, Aleksandrova S S, Votrin I I
Biokhimiia. 1988 Jul;53(7):1163-73.
A scheme for the isolation of Ca,Mg-dependent endonuclease from human spleen lymphocyte nuclei has been developed. The isolation procedure resulted in protein preparations (Mr = 57 kD) possessing an enzymatic activity and stable upon storage for over a period of one year. The enzyme is an endonuclease which predominantly cleaves double-stranded DNA by a mixed single- and double-hit mechanism with the formation of 5'-phosphate and 3'-OH terminal groups. Its maximal activation is induced by Ca2+ plus Mg2+. The enzyme is also active in the presence of Mn2+, Ca2+, Mg2+ and Zn2+ and is inhibited by Co2+. NaCl and KCl (0.15-0.2 M) and p-chloromercuribenzoate (1 mM) also inhibit the enzyme. ATP has no activating effect.
已开发出一种从人脾淋巴细胞核中分离钙、镁依赖性核酸内切酶的方案。分离程序得到了具有酶活性且在储存一年多后仍稳定的蛋白质制剂（Mr = 57 kD）。该酶是一种核酸内切酶，主要通过混合的单链和双链打击机制切割双链DNA，形成5'-磷酸和3'-羟基末端基团。其最大激活由Ca2+加Mg2+诱导。该酶在Mn2+、Ca2+、Mg2+和Zn2+存在时也有活性，并被Co2+抑制。NaCl和KCl（0.15 - 0.2 M）以及对氯汞苯甲酸（1 mM）也抑制该酶。ATP没有激活作用。
