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DNA Polymerases of Myeloma: Template and Primer Specificities of Two Enzymes

Nature New Biology volume 239, pages 173–176 (1972)Cite this article

Abstract

INTEREST in the viral RNA-dependent DNA polymerases1,2 has led to an examination of mammalian DNA polymerases and to the characterization in certain systems of DNA polymerases which can transcribe ribopolymer chains of appropriate ribopolymer-oligodeoxyribopolymer hybrids3,4. The nature of these enzymes and their function in cells are unclear. We have reported the separation, by chromatography on DEAE-cellulose, of the DNA polymerases of the murine myeloma tumour into two separate fractions which we have designated as fractions D-I and D-II (ref. 5). Each of these fractions contains an activity capable of utilizing activated DNA and of transcribing the ribopolymer strand of poly rA oligo dT. We describe here the separation of two DNA polymerase enzymes in fraction D-I.

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Authors and Affiliations

  1. Institute of Microbiology, Rutgers University, New Brunswick, New Jersey, 08903

    FRANCIS J. PERSICO & A. ARTHUR GOTTLIEB

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  1. FRANCIS J. PERSICO
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  2. A. ARTHUR GOTTLIEB
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PERSICO, F., GOTTLIEB, A. DNA Polymerases of Myeloma: Template and Primer Specificities of Two Enzymes. Nature New Biology 239, 173–176 (1972). https://doi.org/10.1038/newbio239173a0

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