DNA POLYMERASE-BETA FROM RAT-LIVER - PURIFICATION, PROPERTIES AND INHIBITORY ANALYSIS OF THE HOMOGENEOUS ENZYME
- 1 December 1985
- journal article
- research article
- Vol. 11 (12) , 1627-1635
Abstract
A simple and reproducible purification procedure of homogeneous DNA polymerase .beta. from rat liver is developed, including sedimentation and saline extraction of rat liver chromatin, chromatography of the extract on DEAE-cellulose, phosphocellulose, Gel Blue A, and DNA sepharose. The purified enzyme isolated with the 8.4% yield proved to be a homogeneous proteins with m.w. 38-40 kDa, specific activity 31 units/g, pI 8.6-8.9. Incorporation of [3H]TTP into activated DNA catalysed by DNA polymerase .beta. was strongly inhibited by dNTP(3''NH2), ddTTP, dNTP(3''F) and slightly inhibited by aCTP and aNTP (3''NH2).This publication has 11 references indexed in Scilit:
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