Purification of a Human Spermatozoal Antigen

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Abstract
A spermatozoal cell membrane antigen was isolated using lithium 3,5-diiodosalicylate as the solubilizing agent. Its apparent MW is 40,500 by gel filtration chromatography and 35,000 by dodecyl sulfate-polyacrylamide gel electrophoresis. Labeling of the antigen with 125I and subsequent radio-immunoprecipitation enabled the evaluation of specific binding of IgG and IgM molecules in sperm-agglutinating and sperm-immobilizing antisera. Adsorption experiments with the purified antigen resulted in significant titer reductions of the same antisera in the microsperm-agglutination and microssperm-immobilization tests. This indicates the presence of an antigen molecule on the human spermatozoa that reacts with IgG and IgM antibodies and with both types of antisera.