[Extracellular ribonuclease from Bacillus pumilus].

N K Struminskaia, V L Ivaĭlovskiĭ, A A Dement'ev, G P Moiseev, Iu A Fedosov, G I Iakovlev
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Abstract

The extracellular ribonuclease (RNAse Bp) was isolated from the cultural medium filtrate of Bacillus pumilus by ammonium sulfate precipitation and two stages of ion-exchange chromatography on carboxymethyl- and phospho-cellulose columns. The amino acid composition and N-terminal amino acid residue have been determined. The kinetic parameters of cleavage reaction of synthetic polynucleotides have been measured. According to their structural homology RNAse Bp has been shown to be similar to RNAses Ba and Bi. Catalytic properties of the enzyme are very close to RNAse Bi.

[细粒芽孢杆菌胞外核糖核酸酶]。
采用硫酸铵沉淀和羧甲基纤维素和磷酸纤维素两级离子交换层析,从短小芽孢杆菌培养基滤液中分离到胞外核糖核酸酶(RNAse Bp)。测定了氨基酸组成和n端氨基酸残基。测定了合成多核苷酸裂解反应的动力学参数。根据其结构同源性,RNAse Bp已被证明与RNAse Ba和RNAse Bi相似。该酶的催化性能与RNAse Bi非常接近。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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