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Purification, Analysis, and Subunits of Myeloma (MOPC 21) DNA-dependent RNA Polymerase A (I) by Polyriboadenylate-Sepharose¹

National Institute of Child Health and Human Development, NIH, Bethesda, Maryland 20014 [S. H. H.], and The Joseph Gottstein Memorial Cancer Research Laboratory, Department of Pathology, University of Washington, Seattle, Washington 98195 [E. A. S.]

DNA-dependent RNA polymerase A (or I) was purified from murine myeloma MOPC 21 by diethylaminoethyl Sephadex chromatography. Further separation from DNA polymerases, protein kinase, and DNA endonuclease was accomplished by polyriboadenylate-Sepharose affinity chromatography followed by gradient centrifugation. Yields following chromatography were 100%, but following gradient centrifugation only 25 to 30% of the activity remained. Addition of low-molecular-weight components increased yields to 50 to 60%. Several species of myeloma polymerase A could be detected, and subunits of 190,000 and 125,000 daltons were identified. No evidence of phosphorylation of the polymerase was found.

¹ These studies were supported in part by USPHS Grants CA 13600, GM 13543, and GM 00100.

² Submitted in partial fulfillment of the requirements for the Ph.D. at the University of Washington.

Received 6/27/75. Accepted 11/17/75.