[Isolation and various properties of beta DNA polymerase from the embryos of the sea urchin Strongylocentrotus intermedius].
DNA-polymerase beta was isolated from embryonic cells of the sea urchin S. intermedius and purified 1040-fold. The molecular weight of the enzyme is 40 000, sedimentation coefficient 3.2S, pI 8.5. The SH-reagent--N-ethylmaleimide--has no appreciable influence on the enzyme activity. The enzyme is thermolabile and needs four deoxyribonucleoside triphosphates, bivalent metal ions (Mg2+ or Mn2+) and primer template for its activity. The maximal activity is observed when a synthetic polymer--poly(dA).oligo(dT) is used. DNA-polymerase performs DNA synthesis via a distributive mechanism. In terms of physico-chemical properties, the enzyme can be related to DNA-polymerases beta.
D000818:Animals; D004256:DNA Polymerase I / Q000302:isolation & purification*; D004625:Embryo, Nonmammalian / Q000201:enzymology*; D005033:Ethylmaleimide; D008970:Molecular Weight; D012617:Sea Urchins; D013379:Substrate Specificity
D004256:DNA Polymerase I; D005033:Ethylmaleimide
Vydelenie i nekotorye svoĭstva DNK-polimerazy beta iz émbrionov morskogo ezha Strongylocentrotus intermedius.