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J. Biochem, 1976, Vol. 80, No. 1 19-26
© 1976 Japanese Biochemical Society

research-article

Purification and Properties of an Alkaline Ribonuclease from the Hepatic Cytosol Fraction of Bullfrog, Rana catesbeiana

Hiroshi NAGANO1, Hiroyuki KIUCHI, Yasuko ABE and Ryoiti SHUKUYA

Department of Biochemistry, Nippon Medical School Sendagi, Bunkyo-ku, Tokyo 113
1Present address: Department of Physiological Chemistry and Nutrition, Faculty of Medicine, The University of Tokyo Hongo, Bunkyo-ku, Tokyo 113.

In the hepatic cytosol fraction of bullfrog, Rana catesbeiana, an alkaline RNase [EC 3. 1. 4. 22] exists in two forms. One is the free form of RNase, which elutes from a carboxymethyl-cellulose column at a concentration of 0.2 M NaCl. The other is a masked or latent form (RNase-RNase inhibitor complex) which is not adsorbed on the carboxymethyl-cellulose column and which can be converted to the free form of RNase by the addition of p-chIoromercuribenzoate. Electrophoretically pure RNase was obtained by the following procedure. The unadsorbed fraction of hepatic cytosol on a column of carboxymethyl-cellulose was treated with p-chloromercuribenzoate and then applied to a second carboxymethyl-cellulose column.

The molecular weight of RNase was determined to be approximately 12,000 by gel filtration and polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. From the results of gel filtration, the molecular weight of the RNase-RNase inhibitor complex was 130,000.

The RNase hydrolyzed poly C, poly C, poly U, and poly I, but not poly A or poly G. When poly C was used as a substrate, 2', 3'-cyclic CMP as an intermediate and 3'-CMP as a final product were identified. The results of amino acid analysis indicated the presence of an unusual component. The general properties of the RNase and the RNase-RNase inhibitor complex are also reported.


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