Identity of the ribonuclease from bovine seminal plasma with ribonuclease BS-1, and its sensitivity to polyvinyl sulphate.
A ribonuclease (RNAase BSD) isolated by us earlier from bovine seminal plasma by DNA-affinity chromatography is shown to be homogeneous on polyacrylamide gel electrophoresis, analytical ultracentrifuge and high performance liquid chromatography. From amino acid analysis, high performance liquid chromatography and enzymatic and physicochemical studies, this enzyme is shown to be identical to RNAase BS-1 reported by D'Alessio et al. ((1972) Eur. J. Biochem. 26, 153-161). Immunological studies support this observation. It has also been shown that, as compared to RNAase A, this enzyme is more sensitive to polyvinyl sulphate inhibition.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D055598:Chemical Phenomena; D002621:Chemistry; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D004722:Endoribonucleases / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D005779:Immunodiffusion; D007700:Kinetics; D008297:Male; D011145:Polyvinyls / Q000494:pharmacology*; D012661:Semen / Q000201:enzymology*
D000596:Amino Acids; D011145:Polyvinyls; C019050:polyvinyl sulfate; D004722:Endoribonucleases; C032523:ribonuclease SPL