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J. Biochem, 1982, Vol. 92, No. 3 855-864
© 1982 Japanese Biochemical Society

research-article

Purification and Properties of Magnesium- and Manganese-Dependent Ribonucleases H from Chick Embryo1

Namiko KITAHARA, Yasuko SAWAI and Kinji TSUKADA

Department of Pathological Biochemistry, Medical Research Institute, Tokyo Medical and Dental University Kandasurugadai, Chiyoda-ku, Tokyo 101

Two RNases H, Mg2+- and Mn2+-dependent RNases H, are present in extracts of chick embryo. These RNases H can be separated by phosphocellulose column chromatography. Mg2+-dependent RNase H was purified over 900-fold and Mn2+-dependent RNase H over 1,700-fold from chick embryo extracts. The molecular weight of the purified Mg2+-dependent RNase H was about 40,000 and of the Mn2+-dependent RNase H about 120,000, when estimated by gel filtration. Mg2+-dependent RNase H exhibits maximal activity at pH 9.5, and requires 15 to 20 mM Mg2+ for maximal activity, whereas Mn2+-dependent RNase H is most active at pH 8.5, and is maximally active at the concentration of 0.4 mM Mn2+, and has some activity with Mg2+. Both enzymes require a sulfhydryl reagent for maximal activity. Mn2+-dependent RNase H was inhibited by o-phenanthroline, pyrophosphate, and those polyamines tested, whereas Mg2+-dependent enzyme was not, although it was inhibited by NaF. Both RNases H liberate a mixture of oligonucleotides with 5'-phosphate and 3'-hydroxyl termini endonucleolytically.

1This investigation was supported in part by a Grant-in-Aid for Cancer Research from the Ministry of Education, Science and Culture of Japan.


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