The predominant protein in human seminal coagulate.
The predominant protein in human seminal vesicle secretion constitutes the structural protein of coagulated semen. This high molecular weight protein (HMW-SV-protein) is stable in seminal vesicle secretion during in vitro storage at 37 degrees C for at least 20 h, but is rapidly cleaved on mixing with prostatic proteases. Seminal coagulate, washed free of soluble components, is dissoluble by 2 to 3 mol/l of guanidine-HCl. Although dithiothreitol added to seminal coagulate does not liquefy the clot, complexes between HMW-SV-proteins are broken up by reduction under denaturing conditions, which suggests that the non-covalent linkages of HMW-SV-proteins are essential in the clot. Prostatic proteases cleave the HMW-SV-protein during liquefaction of ejaculated semen to a series of labile proteins. These proteins are further cleaved to peptides of successively decreasing size after completed liquefaction. The cleavage of the HMW-SV-protein is the major cause of the fast shift of the electrophoretic pattern of seminal proteins if semen is stored without protease inhibitors.
Lilja
H
H
Laurell
C B
CB
D000596:Amino Acids / Q000032:analysis; D003029:Coagulants / Q000032:analysis*; D004587:Electrophoresis, Agar Gel; D006801:Humans; D008297:Male; D008970:Molecular Weight; D011506:Proteins / Q000032:analysis*; D012661:Semen / Q000032:analysis* / Q000201:enzymology; D011503:Transglutaminases / Q000378:metabolism
D000596:Amino Acids; D003029:Coagulants; D011506:Proteins; D011503:Transglutaminases