Seminal plasma biochemistry. III: Characterization of coagulum components

Human seminal plasma components involved in coagulum formation have been isolated by liquefaction and reformation of the coagulum in acidic and neutral buffers, respectively. The SDS-PAGE profile of the isolated coagulum (recoagulum) is similar to that reported for the native coagulum immediately following liquefaction. Thus the recoagulum may be considered to represent the native coagulum. Electrophoresis of the recoagulum under non-denaturing conditions reveals the presence of both positively and negatively charged components. These components are sialoglycoproteins that bind copper. Based on these results, a possible mechanism for coagulum formation and liquefaction is discussed.