STEADY-STATE KINETICS OF MOUSE DNA POLYMERASE-BETA

被引：107

作者：

TANABE, K ^{[1
]}

BOHN, EW ^{[1
]}

WILSON, SH ^{[1
]}

机构：

[1] NCI,BIOCHEM LAB,BETHESDA,MD 20205

来源：

BIOCHEMISTRY | 1979年 / 18卷 / 15期

关键词：

D O I：

10.1021/bi00582a029

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

DNA polymerase β from mouse myeloma has been purified to near homogeneity, and its properties have been examined. The enzyme did not catalyze a detectable level of dNTP turnover, pyrophosphate exchange, pyrophosphorolysis, 3′-exonuclease degradation, or 5′-exonuclease degradation. Steady-state kinetic studies point to an ordered bibi mechanism for the polymerization reaction. Metal activation, which is required for polymerization, did not alter the Km for either the dNTP or the template-primer. © 1979, American Chemical Society. All rights reserved.

引用

页码：3401 / 3406

页数：6

共 26 条

[1]

BAMBARA RA, 1978, J BIOL CHEM, V253, P413

[2] DISTRIBUTIVE NATURE OF ENZYMATIC DNA-SYNTHESIS [J].