• 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).