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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.
H Vonwirth, and
P Frank, and
W Büsen
April 1976,
Proceedings of the National Academy of Sciences of the United States of America,
H Vonwirth, and
P Frank, and
W Büsen
March 1975,
European journal of biochemistry,
H Vonwirth, and
P Frank, and
W Büsen
July 1973,
Proceedings of the National Academy of Sciences of the United States of America,
H Vonwirth, and
P Frank, and
W Büsen
September 1978,
Proceedings of the National Academy of Sciences of the United States of America,
H Vonwirth, and
P Frank, and
W Büsen
October 1980,
The Journal of biological chemistry,
H Vonwirth, and
P Frank, and
W Büsen
June 1982,
The Journal of biological chemistry,
H Vonwirth, and
P Frank, and
W Büsen
October 1961,
Biochimica et biophysica acta,
H Vonwirth, and
P Frank, and
W Büsen
January 1970,
Acta biochimica Polonica,
H Vonwirth, and
P Frank, and
W Büsen
March 1970,
Biochemical and biophysical research communications,
H Vonwirth, and
P Frank, and
W Büsen
November 1989,
European journal of biochemistry,
