来自大肠杆菌K12的一种特异性多聚腺苷酸聚合酶。

A specific polyadenylase from Escherichia coli K12.

作者信息

Antoniades D, Antonoglou O

出版信息

Biochim Biophys Acta. 1977 Feb 16;474(4):609-18. doi: 10.1016/0005-2787(77)90080-6.

Abstract

A polyadenylase, degrading specifically poly(A) sequences was isolated from Escherichia coli K12. The enzyme was purified about 850 times to practically electrophoretic homogeneity. It was free of poly(A) polymerase activity, as well as of the well known E. coli RNAases I and II. It is stimulated by bivalent cations like Mg2+ and Mn2+ and splits poly(A) to 3'-AMP and therefore it can be considered as an exonuclease. The enzyme does not degrade any other ribohomopolymer or RNA.

摘要

从大肠杆菌K12中分离出一种特异性降解聚腺苷酸（poly(A)）序列的聚腺苷酸酶。该酶被纯化了约850倍，达到了几乎电泳纯的程度。它没有聚腺苷酸聚合酶活性，也没有众所周知的大肠杆菌核糖核酸酶I和II。它受到二价阳离子如Mg2+和Mn2+的刺激，能将聚腺苷酸裂解为3'-腺苷酸，因此可被视为一种核酸外切酶。该酶不会降解任何其他核糖均聚物或RNA。