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Extra resources for Chromatin and Chromosomal Protein Research. IV
Biol. G e m . 252, 3082 (1977). 77. , Bell, G. , and Rutter W. , Biochem. Biophys. Res. Commun. 71, 26 (1 976). 78. , Bell, G . , and Rutter, W. , Biochem. Biophys. Res. Commun. 71, 1319 (1976). 79. , Buhler, J. , Sentenac, A. and Fromageot, P. Proc. Natl. Amd. Sci. A. 72, 3034 (1975). 80. Auld, D. , Campino, C. and Valenzuela, P. Biochem. Biophys. Res. Commun. 69,548 (1976). 81. Lattke, L. , FEBS Lett. 65, 288 (1976). Chapter 2 Isolation and Cbaracterixation of D N A Polymerasesfrom Eukatyotic Cells DIPAK K.
G . Enzyme Purity The purity of RNA polymerases is monitored by (a)increase in the specific activity of the enzyme, (b) decrease in the number of protein bands in native or sodium dodecyl sulfate (SDS) gel electrophoresis, and (c) decrease in contaminating nucleolytic, proteolytic, or other activities. All these methods are necessary to fully assess the purity of a preparation. Specificactivities are frequently not comparable from one laboratory to another. The polymerase assay is complex and highly dependent on the natureand state ofthetemplate and the particular assay conditions.
DNA Polymerase-a The class of DNA polymerase that appears to be most abundant in dividing mammalian cells is DNA polymerase-a. These enzymes are of large molecular weight, having a sedimentation coefficient of approximately 68 S. They require sulfhydryl groups for activity as measured by their sensitivity to N-ethylmaleimide. oligo(dT) as a template (3). It is frequently referred to as the “cytoplasmic” DNA polymerase, since it is most easily detected in, and can be readily purified from, cytoplasmic extracts.