Abstract
Summary. A method is described for isolating the acrosomal material from human spermatozoa. Ejaculated spermatozoa are washed in a balanced salt solution containing glucose and dextran and are then rapidly frozen in liquid nitrogen, thawed at room temperature and the supernatant is collected after centrifugation. Electron microscope observations on the sperm pellet indicate a fairly selective removal of the acrosomal content with only minor damage to other parts of the spermatozoon. The presence of trypsin-like enzyme activity in the supernatant material thus obtained, was demonstrated by its ability to digest BAEE and TAME and by inhibition of this activity with soybean trypsin inhibitor and TLCK. Blood serum and seminal plasma were both found to contain a potent inhibitor of this enzyme activity. A reasonably consistent activity per mg of `acrosomal protein' makes it improbable that the enzymatic activity is found in an inhibited state in ejaculated spermatozoa.

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