Purification and Properties of Seminal Vesicle Ribonucleases

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1) Two ribonuclease [EC 2. 7. 7. 16], RNases Vs1 and Vs2, were isolated from bovine seminal vesicles. They were purified 380 and 460 fold respectively, by CM-cellulose, Sephadex G-75 and P-cellulose column chromatographies. Both enzymes were homo-geneous on gel electrophoresis.<br> 2) The molecular weights of RNases Vs1 and Vs2 were 25, 500 and 13, 000, respec-tively as determined by means of gel filtration. The latter enzyme was different from bovine pancreatic RNase A on gel electrophoresis.<br> 3) RNases Vs1 and Vs2 were very similar to RNase A in respect of base specificity, pH optimum, stability and behavior against heavy metal ions, such as Zn2+ and Cu.2+ 4) Amino acid composition of RNase Vs1 was reported. The amino-and carboxyl-terminal amino acids of the enzyme were lysine and valine, respectively and coin-cided with those of bovine pancreatic RNase A.

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