title: [Electrophoretic study of the protein composition of human seminal vesicle secretion].
abstract: The SDS-PAGE and two-dimensional reductived electrophoretic study of the liquid aspirated from human seminal vesicles showed that this medium contains high molecular weight proteins (greater than 150 kDa). In addition to these high molecular weight proteins, native seminal vesicle secretion is characterised by the presence of a large 47.4 kDa protein band corresponding to seminogelin, described by Lilja. The high molecular weight proteins actually correspond to associations of three types of protein subunits with molecular weights of 75-76, 63-64 and 47-48 kDa, which represent the structural elements of the coagulum; one of these subunits consists of seminogelin. Seminal vesicle secretion contains very little or no proteolytic enzymes, so that its protein composition remains stable even after incubation for 24 hours.
authors.affiliation: Faculté de Médecine, Laboratoire d'Embryologie, Strasbourg.
authors.forename: D
authors.initials: D
authors.lastname: Montagnon
mesh_terms: D001826:Body Fluids / Q000737:chemistry* / Q000378:metabolism; D004586:Electrophoresis; D006801:Humans; D008297:Male; D008970:Molecular Weight; D011506:Proteins / Q000032:analysis*; D012669:Seminal Vesicles / Q000378:metabolism*
chemical_list: D011506:Proteins
vernacular_title: Etude électrophorétique de la composition protéique de la sécrétion vésiculaire humaine.