Phosphorylation of sperm-binding proteins from seminal vesicle secretion by sperm surface protein kinase.
Rat seminal vesicle secretion does not demonstrate protein kinase activity, either towards endogenous or exogenous proteins. When epididymal sperm were incubated in vitro with seminal vesicle secretion, three prominent secretory proteins were bound to the sperm. Two of these proteins were highly phosphorylated. Thus, selected sperm-binding proteins from accessory gland secretions are phosphorylated by sperm surface protein kinases.
Wilson
M J
MJ
Research Service, VA Medical Center, Minneapolis, Mn.
D000818:Animals; D002352:Carrier Proteins / Q000378:metabolism*; D000242:Cyclic AMP / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D006358:Hot Temperature; D066298:In Vitro Techniques; D008297:Male; D008565:Membrane Proteins / Q000378:metabolism; D010766:Phosphorylation; D047428:Protein Kinase Inhibitors; D011494:Protein Kinases / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D029589:Seminal Plasma Proteins; D012669:Seminal Vesicles / Q000378:metabolism*; D013094:Spermatozoa / Q000201:enzymology*
D002352:Carrier Proteins; D008565:Membrane Proteins; D047428:Protein Kinase Inhibitors; D029589:Seminal Plasma Proteins; C425042:spermadhesin; D000242:Cyclic AMP; D011494:Protein Kinases