Purification and Properties of Seminal Vesicle Ribonucleases
- 1 January 1971
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 69 (4) , 683-697
- https://doi.org/10.1093/oxfordjournals.jbchem.a129518
Abstract
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 homogeneous on gel electrophoresis. 2) The molecular weights of RNases Vs1 and Vs2 were 25,500 and 13,000, respectively as determined by means of gel filtration. The latter enzyme was different from bovine pancreatic RNase A on gel electrophoresis. 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 coincided with those of bovine pancreatic RNase A.Keywords
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