A high ribonuclease activity has been detected in bull seminal plasma; two major fractions (RNAase BS-1 and RNAase BS-2) have been identified, which are responsible for such activity and one of the two, RNAase BS-I, has been purified and crystallized.It has a molecular weight of 29000, an isoelectric point a t pH 10.3 and A:'&, a t 278 nm is 4.65, The amino acid composition has been determined, its main features being a high content of basic residues, the absence of tryptophan and cysteine, and the presence of 18 half-cystine residues.The enzyme is produced by the seminal vesicles, and occurs in seminal plasma as a free, soluble component.For some years we have been studying the ribonuclease activity which we have found to occur in high concentration in the seminal plasma of the bull, with general properties similar to those of bovine pancreatic ribonuclease. We have seen that such activity is the result of a t least two enzymes and our research has been focused on the major component. We wish to give here a full report of the purification procedure of this enzyme (RNAase BS-I), with its amino acid composition and the relevant physicochemical properties, while the following paper [l] will deal with the mechanism of action.Partial results of our research have already been published [2-61.