高纯度肋生弧菌多核苷酸磷酸化酶的制备及性质

Preparation and properties of highly-purified Vibrio costicola polynucleotide phosphorylase.

作者信息

Harry K, Sharma N, Fitt P S

出版信息

Biochim Biophys Acta. 1985 Mar 22;828(1):29-38. doi: 10.1016/0167-4838(85)90005-6.

Abstract

Vibrio costicola polynucleotide phosphorylase (polyribonucleotide: orthophosphate nucleotidyltransferase, EC 2.7.7.8) has been purified to electrophoretic homogeneity. It has an approximate molecular weight of 220 000 and consists of identical subunits with an approximate molecular weight of 72 000. The enzyme appears to be a fairly typical polynucleotide phosphorylase with respect to its pH optima, substrate specificity and requirement for a divalent cation cofactor. However, the effect of salt concentration on its physiologically important phosphorolysis activity suggests that it is a moderately halophilic enzyme, able to function at the intracellular ionic strength of the bacterium. In addition, its ADP polymerization activity is remarkably stimulated by polylysine.

摘要

肋生弧菌多核苷酸磷酸化酶（聚核糖核苷酸：正磷酸核苷酸基转移酶，EC 2.7.7.8）已被纯化至电泳纯。它的分子量约为220000，由分子量约为72000的相同亚基组成。就其最适pH值、底物特异性和对二价阳离子辅因子的需求而言，该酶似乎是一种相当典型的多核苷酸磷酸化酶。然而，盐浓度对其生理上重要的磷酸解活性的影响表明它是一种中度嗜盐酶，能够在细菌的细胞内离子强度下起作用。此外，其ADP聚合活性受到聚赖氨酸的显著刺激。