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A Deoxyribonuclease from Mammary Tumours of C3H Mice preferentially hydrolysing Heat-denatured DNA

Abstract

ENZYMES hydrolysing heat-denatured DNA exclusively, or at a faster rate than native DNA, have been reported in the literature. Two are of bacterial origin1,2, two of mammalian origin3,4, and one from the venom of Viperalebotina5. Burdon, Smellie and Davidson identified one such enzyme, in extracts of rat liver, as being an inhibitor of the synthesis of DNA by hydrolysing the DNA primer in the DNA polymerase reaction4. If the function of these enzymes is to destroy DNA templates, their significance is obvious, even though it would be hard to assign such a role to the extracellular micrococcal nuclease1, or to the gurza venom enzyme5.

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References

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GEORGATSOS, J., SYMEONIDIS, A. A Deoxyribonuclease from Mammary Tumours of C3H Mice preferentially hydrolysing Heat-denatured DNA. Nature 206, 1362–1363 (1965). https://doi.org/10.1038/2061362a0

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  • DOI: https://doi.org/10.1038/2061362a0

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