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J. Biochem, 1974, Vol. 76, No. 6 1319-1325
© 1974 Japanese Biochemical Society

research-article

Reoxidation of Reduced Ribonuclease from Bovine Seminal Vesicles

Masachika IRIE and Akie TSUBOTA

Department of Microbiology, Hoshi College of Pharmacy Ebara 2-4-41, Shinagawa-ku, Tokyo 142

  1. Ribonuclease [EC 3.1.4.22 [EC] [EC] ] from bovine seminal vesicles, having a molecular weight of 25,500, was reduced with 2-mercaptoethanol. The reduced RNase Vs1 was inactive enzymatically and its molecular weight was about 14,000.
  2. When the reduced RNase Vs1 was reoxidized in the presence of air, enzymatic activity reappeared and became almost constant after about 200 min incubation.
  3. Electrophoresis of reoxidized reduced RNase Vs1 on polyacrylamide gel containing sodium dodecyl sulfate (SDS) showed two protein species, one of which coincided with native RNase Vs1 and the other with reduced RNase Vs1.
  4. Gel filtration of reoxidized reduced RNase Vs1 indicated the presence of two enzymatically active species.
  5. The faster-moving fraction of reoxidized reduced RNase Vs1 on Sephadex G-75 column chromatography was indistinguishable from native RNase Vs1 on disc electrophoresis, column chromatography on carboxymethyl-cellulose (CM-cellulose), specific activity and Michaelis constant measured using 2', 3'-cyclic CMP as a substrate.
  6. Reoxidized reduced RNase Vs1 was indistinguishable serologically from native RNase Vs1 when tested by Ouchterlony double diffusion analysis.


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