Biochemical and immunological properties of the DNA polymerase and RNAase H activities of purified feline leukemia virus reverse transcriptase

Cancer Letters
H M Rho, R C Gallo

Abstract

Feline leukemia virus DNA polymerase was purified by ion-exchange and nucleic acid affinity chromatographies. The enzyme consists of a single polypeptide chain of mol. wt. approx. 72,000 as determined by both glycerol density gradient centrifugation and SDS-polyacrylamide gel electrophoresis. The preferred divalent cation for DNA synthesis is Mn2+ on a variety of template-primers, and its optimum concentration appears to be significantly lower than reported results of other mammalian type-C viral enzymes. The purified enzyme also contained RNAase H activity. Both DNA polymerase and RNAase H activities appear to reside on the same molecule as demonstrated by the copurification of both activities through various purification steps. The divalent cation requirement for maximum activity of RNAase H is also similar to that of the DNA polymerase. RNAase H without detectable polymerase activity was generated by a limited chymotrypsin digestion of the purified reverse transcriptase. This RNAase H activity was inhibited equally effectively as RNAase H in the intact reverse transcriptase by antisera prepared against reverse transcriptase of feline leukemia virus. These results indicate that the RNAase H catalytic activity of reverse trans...Continue Reading

References

May 1, 1977·Journal of Virology·J M KrakowerS A Aaronson
Dec 11, 1978·Biochimica Et Biophysica Acta·M G SarngadharanR C Gallo
Sep 22, 1972·Science·E M ScolnickG J Todaro

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Citations

Jun 1, 1988·AIDS Research and Human Retroviruses·P GalloL Chieco-Bianchi
Mar 1, 1990·AIDS Research and Human Retroviruses·A De RossiL Chieco-Bianchi
Jun 1, 1990·Veterinary Microbiology·H Lutz
May 1, 1995·Veterinary Immunology and Immunopathology·R Hofmann-LehmannH Lutz
Apr 4, 2012·Viruses·Stephen J O'BrienJill Pecon-Slattery

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