Molecular characterization of human sperm coating antigen recognized by the human monoclonal sperm immobilizing antibody (H6-3C4).
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A human monoclonal antibody (MAb) with strong sperm immobilizing and agglutinating activities was prepared from a spent culture medium of a human-mouse heterohybridoma (H6-3C4) established in our laboratory. The molecular natures of the antigen corresponding to the MAb (H6-3C4) were studied. A large amount of the antigen was present in human seminal plasma (HSP) as a soluble substance. When HSP precipitated with saturated ammonium sulfate was fractionated by gel filtration on Sephacryl S-300 column, most of the antigen activities was eluted in the void fraction as large macromolecules (over 670kD). However, when the void fraction was subjected to sodium dodecylsulfated polyacrylamide gel electrophoresis (SDS-PAGE) in either reducing or non-reducing conditions and transblotted to a nitrocellulose membrane (Western blotting), the antigen was detected as a broad immunostaining band around the 20kD region. Further fractionation of the void fraction from Sephacryl S-300 chromatography by Fast Protein Liquid Chromatography (FPLC) on ProRPC HR5/2 column revealed that the antigenic molecule was eluted as a single peak of a substance with a high hydrophobicity.
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