Electrophoretic Fractionation of Bovine Acrosomal Proteins and Proteinase

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Abstract
Acrosomal proteins from the spermatozoa of four bulls were separated using discontinuous electrophoretic techniques to fractionate both anodic (pH 9.5 system) and cathodic (pH 4.3 system) components. A zymographic technique suitable for visualization of trypsin-like proteinase activity after electrophoresis on acrylamide gels was used to localize proteinase (acrosin) activity in three of 12 protein fractions detected in acrosomal materials isolated from ejaculated bovine spermatozoa. All three acrosin fractions, designated A-1, A-2, and A-3, showed optimum activity at pH 7.5 with an additional peak of activity at pH 5.5. The acrosin fractions possessed electrophoretic mobilities distinctly different from that of purified bovine pancreatic trypsin, but were inhibited by the antitrypsin reagent, tosyl-L-lysine chloromethyl ketone HCl (TLCK). The relative electrophoretic mobilities of some protein fractions present in acrosomal materials suggested that they were originally components of the seminal plasma.

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