Steady-state kinetics of mouse DNA polymerase .beta.
- 1 July 1979
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 18 (15), 3401-3406
- https://doi.org/10.1021/bi00582a029
Abstract
DNA polymerase .beta. from mouse myeloma MOPC-104E was purified to near homogeneity, and its properties were examined. The enzyme did not catalyze a detectable level of dNTP (deoxynucleoside 5''-triphosphate) turnover, PPi 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.Keywords
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