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Apparent specificity of bovine seminal ribonucleases can depend on the conditions used for the isolation of substrate.

RNAase SPL, a ribonuclease isolated earlier from bovine seminal plasma, was shown to possess the ability to produce large acid-insoluble fragments of Mg(2+)-containing RNA in a limit digest. The factor which could be responsible for this apparent specificity has been identified as polyvinyl sulphate; it has been shown that polyvinyl sulphate inhibits RNAase SPL at much lower concentrations than required for RNAase A. The earlier results are now reinterpreted based on this effect of polyvinyl sulphate, thus providing a plausible explanation for RNAase SPL's apparent specificity. RNAase SPL has been shown to be a mixture of two ribonucleases, RNAase SPL I and RNAase SPL II. RNAase SPL I is like RNAase A in its activity while RNAase SPL II, the major ribonuclease in seminal plasma, appears to be identical to RNAase BS1.