
doi: 10.1007/bf00266405
pmid: 2185199
A monoclonal antibody, designated mAb P86/5, was generated by immunization of female Balb/c mice with a membrane vesicle fraction composed of the outer acrosomal membrane and plasma membrane (PM-OAM). As determined by fluorescence microscopy and electron microscopy P86/5 recognizes a sperm plasma membrane antigen that is restricted to the sperm head. In intact spermatozoa the P86/5-antigen is distributed over the surface of the sperm head with the exception of the rostral region. By comparing the antibody binding pattern generated at 4 degrees C and 25 degrees C, it could be shown that the P86/5-antigen is capable to diffuse freely within the cell membrane overlying the acrosome whereas its lateral mobility is restricted to the post-acrosomal region. The P86/5-antigen had a molecular weight of about 78 kDa as revealed by SDS-PAGE and western blotting. The glycoprotein nature of the P86/5-antigen was established by lectin affinity chromatography.
Male, Membrane Glycoproteins, Swine, Cell Membrane, Antibodies, Monoclonal, Fluorescent Antibody Technique, Spermatozoa, Microscopy, Electron, Antigens, Surface, Animals
Male, Membrane Glycoproteins, Swine, Cell Membrane, Antibodies, Monoclonal, Fluorescent Antibody Technique, Spermatozoa, Microscopy, Electron, Antigens, Surface, Animals
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