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Poly(A) Polymerase of Bovine Lymphosarcoma¹

Departments of Biochemistry [A. A. K.] and Pathology [S. M. M., J. J. F.], School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19174

Poly(A) polymerase has been extensively purified from low-salt extracts of bovine lymphosarcoma. The enzyme is Mn²⁺ dependent, requires an oligonucleotide or RNA primer, incorporates only adenosine triphosphate, and is inhibited by other ribonucleotides or deoxynucleotides. Oligoadenylate and ribosomal RNA are good primers for the enzyme; transfer RNA and poly(A) are poor. RNA transcribed in vitro by homologous RNA polymerase is an efficient primer.

The properties of the enzyme are similar to the properties of the Mn²⁺-activated poly(A) polymerase of calf thymus. Approximately the same amount of enzyme appears to be present in lymphosarcoma and calf thymus.

¹ This investigation was supported by Grant 2-R01-GM-10390 from the NIH, USPHS. Support for maintenance of the herd with a high incidence of lymphosarcoma came from USPHS Cancer Center Grant 1-P01-CA-14193-01, USPHS Contract PH-43-S-1013 within the Virus Cancer Program of the National Cancer Institute, and USPHS Grant 5-PO-6-RR-00182.

² Supported by Medical Scientist Training Program NIH Training Grant 5T05 GM-02046.

Received 11/11/74. Accepted 1/23/75.

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