Purification and initial characterization of proacrosins from guinea pig testes and epididymal spermatozoa.
Previous studies showed that interspecies differences in proacrosin size may exist. We purified guinea pig proacrosins, one from testes and two from epididymal spermatozoa, by gel filtration and cation exchange at acidic pH. Final purification was by cation exchange at pH 8.0 in 6 M urea. Testis proacrosin migrated with 62,000 Mr in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). One sperm proacrosin migrated with 43,000 Mr, and the other as a 56,000/54,000 Mr doublet in SDS-PAGE. These results represent the first purification of three forms of proacrosin from one species, and the first purification to homogeneity of a 43,000 Mr proacrosin. The proacrosins autoactivate at pH 8.0 with similar kinetics, copurify until the last purification step, and share antigenic determinants. It is possible that the sperm proacrosins are derived from the testis proacrosin, perhaps by proteolysis. The sizes of the three guinea pig proacrosins reported in this study are similar to those reported for proacrosins from other species. Apparent interspecies differences in proacrosin size may be primarily a question of which of at least three possible forms of the zymogen predominates in a species.
D000176:Acrosin / Q000302:isolation & purification*; D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D004792:Enzyme Precursors / Q000302:isolation & purification*; D004822:Epididymis / Q000032:analysis; D006168:Guinea Pigs; D008297:Male; D008970:Molecular Weight; D012697:Serine Endopeptidases / Q000302:isolation & purification*; D013094:Spermatozoa / Q000032:analysis*; D013737:Testis / Q000032:analysis*
D004792:Enzyme Precursors; D012697:Serine Endopeptidases; C022438:proacrosin; D000176:Acrosin