PRIMARY STRUCTURE OF RIBONUCLEASE FROM BACILLUS-INTERMEDIUS 7P
PRIMARY STRUCTURE OF RIBONUCLEASE FROM BACILLUS-INTERMEDIUS 7P
复制标题
DOI：
10.1016/0014-5793(79)80056-3
复制
发表时间：
1979-01-01
期刊：
影响因子：
3.5
通讯作者：
SEVERIN, ES
中科院分区：
文献类型：
--
作者：
APHANASENKO, GA;DUDKIN, SM;SEVERIN, ES
关于核糖核酸酶的结构与功能之间关系的研究主要是用核糖核酸酶A [1]进行的，在较小程度上用核糖核酸酶Tr [2]进行的。细菌核糖核酸酶在这方面的研究明显较少。到目前为止，只有一种细菌核糖核酸酶，即B的核糖核酸酶的一级结构和一些理化性质被研究。已建立[3-S]。本研究的目的是确定的胞外核糖核酸酶的一级结构的芽孢杆菌intennedius，菌株7 P。RNA酶催化RNA分解为以3 '-磷酸和1 s为终止的寡核苷酸，主要对RNA分子的嘌呤碱基具有特异性[6]。核苷3 '* 3'-磷酸和二核苷磷酸对thrs酶的作用是完全耐受的。[7]中描述了均相RNA酶的大规模制备和该酶的一些特性。
Stmhes on the relation between the structure and function of RNases have been carried out mainly with RNase A [1] and to a lesser extent wrth RNase Tr [2]. Bacterial RNases have been significantly less stu&ed m this respect. Up to now, the primary structure and some physrcochemical properties of only one bacterial RNase, namely the RNase of B. amyloliquefaciens, have been established [3-S]. The purpose of this study was to determine the primary structure of the extracellular RNase of Bacillus intennedius, strain 7P. The RNase catalyses the breakdown of RNA to oligonucleotides termmating in 3’-phosphate and 1s mainly specific towards the purine bases of the RNA molecule [6]. Nucleoside3’* 3’-phosphates and dinucleoside phosphates are completely renstant to the action of thrs enzyme. The large scale preparation of the homogeneous RNase and some characteristics of this enzyme were described m [7].