An Inhibitor of DNA Polymerase Produced by Tumor Cells

  • A. A. Gottlieb
  • A. H. Smith
  • O. J. Plescia
  • D. E. Nicholson
  • S. Bowers
  • E. Pankuch
  • D. Berkoben

Abstract

We have previously described the isolation and partial characterization of several DNA polymerases from the murine myeloma, MOPC 21 (1,2). In particular, we have called attention to a distinct enzyme from this line of cells (R-1 polymerase), which has the ability to utilize the synthetic polynucleotide duplex poly rA:oligo(dT)12–18 very efficiently. In this regard, R-1 polymerase resembles reverse transcriptase from the Rauscher murine leukemia virus, but it can be readily distinguished from the latter by its sedimentation coefficient and isolectric point. A summary of the comparative properties of the R-1 polymerase and the reverse transcriptase from the Rauscher murine leukemia virus are listed in Table 20-1.

Keywords

Multiple Myeloma Ammonium Sulfate Murine Leukemia Virus Sedimentation Coefficient Syngeneic Mouse 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag New York Inc. 1975

Authors and Affiliations

  • A. A. Gottlieb
  • A. H. Smith
  • O. J. Plescia
  • D. E. Nicholson
  • S. Bowers
  • E. Pankuch
  • D. Berkoben

There are no affiliations available

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