MAJOR GOAT SPERM 105 KDA MATURATION ANTIGEN - PURIFICATION, CHARACTERIZATION, AND EFFECT OF ITS ANTISERUM ON ACROSIN ACTIVITY

A ConA binding membrane glycoantigen of 105 kDa molecular mass was pur ified from mature goat sperm by ion exchange and gel filtration chroma tography. Of the detergents examined, the anionic deoxycholate was fou nd to be highly effective in maximum solubilization of this sperm memb rane antigen (SMA2). The analysis of the saccharide components by gas liquid chromatography revealed that the 105 kDa antigen (SMA2) contain ed the highest amount of mannose, followed by galactose and glucose in a ratio of 4:3:1. One amino sugar, N-acetylglucosamine, was also foun d to be present in the polysaccharide branching of the SMA2 antigen. T he internal sulfydryl linkage is essential for the maintenance of the protein backbone of 105 kDa antigen. The antigen selectively resides o n the anterior head of goat sperm. The binding of anti-SMA2 antibody t o the integrated mature goat spermatozoa inhibited the release of acro sin after the induction of spermatozoa with Ca-ionophore.