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J. Biol. Chem., Vol. 264, Issue 36, 21491-21497, Dec, 1989
NF Insdorf and DF Bogenhagen
DNA polymerase gamma has been purified over 10,000-fold from mitochondria
of Xenopus laevis ovaries. We have developed a novel technique which
specifically photolabels DNA polymerases. This procedure, the DNA
polymerase trap, was used to identify a catalytic subunit of 140,000 Da
from X. laevis DNA polymerase gamma. Additional catalytically active
polypeptides of 100,000 and 55,000 Da were identified in the highly
purified enzyme. These appear to be products of degradation of the
140,000-Da subunit. The DNA polymerase trap, which does not require large
amounts of enzyme or renaturation from sodium dodecyl sulfate, is an
alternative to the classic "activity gel."
DNA polymerase gamma from Xenopus laevis. I. The identification of a high molecular weight catalytic subunit by a novel DNA polymerase photolabeling procedure
Department of Pharmacological Sciences, State University of New York, Stony Brook 11794-8651.
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