Presence of DNA polymerase in lymphosarcoma in northern pike (Esox lucius)

• Published in: Cancer research (Chicago, Ill.) Vol. 37; no. 9; p. 3214
• Main Authors: Papas, T S, Pry, T W, Schafer, M P, Sonstegard, R A
• Format: Journal Article
• Language: English
• Published: United States 01-09-1977
• Subjects: Animals; DNA-Directed DNA Polymerase - isolation & purification; DNA-Directed DNA Polymerase - metabolism; Fish Diseases - enzymology; Fishes; In Vitro Techniques; Isoelectric Focusing; Lymphoma, Non-Hodgkin - enzymology; Lymphoma, Non-Hodgkin - veterinary; Nucleic Acid Synthesis Inhibitors; Oncogenic Viruses - enzymology; Polynucleotides - metabolism; Pyran Copolymer - pharmacology; Reverse Transcriptase Inhibitors; RNA-Directed DNA Polymerase - isolation & purification; RNA-Directed DNA Polymerase - metabolism; Seasons; Temperature
• ISSN: 0008-5472

Northern poke lymphosarcoma DNA polymerase was partially purified from particulate fractions banding at 1.15 to 1.16 g/ml from homogenates prepared from frozen necropsies of tumor-bearing pike. The enzyme behaves as a typical reverse transcriptase, in that it prefers ribotemplates to deoxytemplates. The isoelectric point (pl 5.5) is similar to that of avian myeloblastosis virus polymerase. The pike enzyme elutes from a phosphocellulose column at 0.22 M potassium phosphate, the same as avian myeloblastosis virus DNA polymerase. The enzyme activity is inhibited by pyran, a specific inhibitor of viral DNA polymerases. The most striking difference between the pike lymphoma polymerase and the other viral DNA polymerases tested is the low maximum temperature of 20 degrees, compared to 30 degrees for Rauscher leukemia virus polymerase and 38 degrees for avian myeloblastosis virus and Rous sarcoma virus.