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An improved method for isolation of tritium-labelled auto-antigen I of the human sperm membrane
The isolation of tritium-labelled auto-antigen I of the human sperm membrane can be improved by including a gel chromatography step on a Sephadex G-200 column in the isolation procedure. The antigen was isolated from tritium-labelled spermatozoa by detergent solubilization, lectin affinity chromatography, gel chromatography and indirect immunoprecipitation. The gel chromatography removed the majority of material which binds non-specifically in the indirect immunoprecipitation and which had complicated the electrophoretic analysis of the isolated antigen. The auto-antigen was found to have a molecular weight greater than 150,000 and to exhibit an electrophoresis pattern of six polypeptide chains with molecular weights of 21,000, 32,000, 41,000, two around 77,000, and 120,000.
The isolation of tritium-labelled auto-antigen I of the human sperm membrane can be improved by including a gel chromatography step on a Sephadex G-200 column in the isolation procedure. The antigen was isolated from tritium-labelled spermatozoa by detergent solubilization, lectin affinity chromatography, gel chromatography and indirect immunoprecipitation. The gel chromatography removed the majority of material which binds non-specifically in the indirect immunoprecipitation and which had complicated the electrophoretic analysis of the isolated antigen. The auto-antigen was found to have a molecular weight greater than 150,000 and to exhibit an electrophoresis pattern of six polypeptide chains with molecular weights of 21,000, 32,000, 41,000, two around 77,000, and 120,000.