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Calf thymus ribonuclease H IIa activity lacks ribonuclease H specificity

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Summary

Less purified fractions of ribonuclease H IIa activity of calf thymus display divalent cation-dependent ribonuclease H activity and divalent cation-independent ribonuclease activity. Because the ratio of the two enzyme activities does not change during successive chromatographic procedures, we suggest that ribonuclease H IIa activity is indeed able to degrade both ssRNA and the RNA moiety of RNA·DNA-hybrids. Ribonuclease H IIa activity can therefore be differentiated from calf thymus ribonuclease H I and H IIb by its lack of ribonuclease H specificity. The native molecular mass of ribonuclease H IIa activity is between 23 and 28 kDa. Under denaturing conditions a 23 kDa-protein band copurifies with the enzyme activity suggesting that this enzyme is monomeric.

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  1. Lehrstuhl für Allgemeine Genetik, Biologisches Institut, Universität Tübingen, Auf der Morgenstelle 28, D-7400, Tübingen, Federal Republic of Germany

    H. Vonwirth, P. Frank & W. Büsen

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  1. H. Vonwirth
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  2. P. Frank
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  3. W. Büsen
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Vonwirth, H., Frank, P. & Büsen, W. Calf thymus ribonuclease H IIa activity lacks ribonuclease H specificity. Experientia 46, 319–321 (1990). https://doi.org/10.1007/BF01951777

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  • DOI: https://doi.org/10.1007/BF01951777

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