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- W2000557169 abstract "Abstract Murine mammary tumor virus (MuMTV) DNA polymerase was purified by affinity chromatography on polycytidylate-agarose followed by phosphocellulose ion-exchange chromatography. The resulting enzyme preparation contained two major polypeptides, of 85,000 and 50,000 daltons as determined by SDS-polyacrylamide gel electrophoresis, and appeared, except for low levels of RNase H, free of DNase and RNase activity. The molecular weight of the purified native enzyme as determined by velocity sedimentation, was approx. 108,000. MuMTV DNA polymerase appears to be a zinc metalloenzyme and requires at least one reduced sulfhydryl group for the expression of catalytic activity. Apparent K m values determined for synthetic template-primers and deoxynucleoside triphosphates were 1 μg/ml and 10–12 μ M , respectively. Examination of the optimal biochemical conditions for DNA synthesis on a variety of template-primers revealed that Mg 2+ was the preferred divalent cation for DNA synthesis. Mn 2+ could partially substitute for Mg 2+ , although it inhibited DNA synthesis when added in the presence of Mg 2+ . MuMTV DNA polymerase exhibited a preference for (dC) n ·(dG) 12−18 among all the synthetic template-primers tested. Activated DNA was preferred as a heteropolymeric template for DNA synthesis when compared with viral 70 S RNA with either endogenous primers or with (dT) 10 as a primer. Rates of heat inactivation of the MuMTV DNA polymerase were found to vary depending upon the template-primer used to measure that inactivation." @default.
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- W2000557169 date "1976-05-01" @default.
- W2000557169 modified "2023-09-23" @default.
- W2000557169 title "Purification and properties of murine mammary tumor virus DNA polymerase" @default.
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- W2000557169 doi "https://doi.org/10.1016/0042-6822(76)90109-4" @default.
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