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