人胎盘核糖核酸酶抑制剂在大肠杆菌中的表达。

Expression of human placental ribonuclease inhibitor in Escherichia coli.

作者信息

Lee F S, Vallee B L

机构信息

Department of Biological Chemistry, Harvard Medical School, Boston, Massachusetts 02115.

出版信息

Biochem Biophys Res Commun. 1989 Apr 14;160(1):115-20. doi: 10.1016/0006-291x(89)91628-8.

DOI:10.1016/0006-291x(89)91628-8

PMID:2653313

Abstract

Human placental ribonuclease inhibitor (PRI) has been expressed in and isolated from Escherichia coli. Its apparent molecular weight, immunoreactivity and amino acid composition are virtually identical with those of native PRI. It inhibits the enzymatic activities of either angiogenin, a blood vessel inducing protein homologous to pancreatic RNase (RNase A), or RNase A in a stoichiometry of 1:1. Recombinant PRI binds to angiogenin and RNase A with Ki values of 2.9 x 10(-16) M and 6.8 x 10(-14) M, respectively, comparable to the affinities of native PRI for these enzymes. Thus, these results confirm that PRI inhibits angiogenin more effectively than RNase A.

摘要

人胎盘核糖核酸酶抑制剂（PRI）已在大肠杆菌中表达并分离出来。其表观分子量、免疫反应性和氨基酸组成与天然PRI几乎相同。它以1:1的化学计量比抑制血管生成素（一种与胰腺核糖核酸酶（RNase A）同源的血管诱导蛋白）或RNase A的酶活性。重组PRI与血管生成素和RNase A的结合常数（Ki值）分别为2.9×10⁻¹⁶ M和6.8×10⁻¹⁴ M，与天然PRI对这些酶的亲和力相当。因此，这些结果证实PRI对血管生成素的抑制作用比RNase A更有效。