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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1973 Jul;70(7):2117–2121. doi: 10.1073/pnas.70.7.2117

Characterization and Separation of Viral DNA Polymerase in Mouse Milk

R S Howk 1,2,3, L A Rye 1,2,3, L A Killeen 1,2,3, E M Scolnick 1,2,3, W P Parks 1,2,3
PMCID: PMC433678  PMID: 4124683

Abstract

Two DNA polymerase with properties of viral RNA-directed DNA polymerase can be found in RIII mouse milk. One enzyme is the polymerase of type-C viruses; this enzyme prefers manganese to magnesium with poly(rA)·oligo(dT) as synthetic template, is inhibited by specific sera, and has an apparent molecular weight of 70,000. Milk from BALB/c and NIH Swiss mice contain a vast predominance of this type-C enzyme. The other DNA polymerase from RIII mouse milk prefers magnesium to manganese, is not inhibited by type-C antipolymerase serum, and appears larger on gel chromatography than the type-C viral polymerase. Its presence in milk from RIII mice and absence from milk of mice with low content of mammary tumor virus correlates to the relative degree of type-B virus expression in these mice. The DNA polymerase of Mason-Pfizer monkey virus, isolated from a rhesus monkey breast tumor, also has a marked preference for magnesium with poly(rA)·oligo(dT), is not immunologically related to primate type-C viruses, and appears larger than the gibbon type-C enzyme on gel chromatography.

Keywords: type-B and type-C virus, Mason-Pfizer monkey virus, gibbon type-C virus

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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