Molecular structure of human seminal coagulum: the role of proteolysis.

The techniques of SDS-polyacrylamide slab gel electrophoresis and a sensitive fluorescamine-based method were used to study autoproteolysis of human seminal coagulum at various pH. The major protein bands of 72 and 55 Kd were optimally degraded at pH 7.5. Degradation at pH 3.5 was preceded by a lag period of 30 min. When the seminal coagulum was incubated for 5 min at pH 7.5 and then adjusted to pH 3.5, degradation was more rapid and complete than at pH 3.5 only. Autoproteolytic degradation product of discreted sizes were obtained when compared with degradation in the presence of pronase.