Binding of seminalplasmin to the plasma and acrosomal membranes of bovine spermatozoa. Fluorescence studies on the changes in the lipid-phase fluidity.
The binding of seminalplasmin, a protein secreted by the accessory sex glands of bull, to the plasma and outer acrosomal membrane of bovine spermatozoa was studied using three different fluorescent probes. 8-Anilino-1-naphthalenesulfonate fluorescence, pyrene excimer fluorescence and diphenylhexatriene fluorescence polarisation studies indicate that seminalplasmin binds to the spermatozoal membranes, and leads to an increase in the fluidity of both the plasma and the acrosomal membranes. Calcium was found to have no influence on the interaction of seminalplasmin with the spermatozoal membranes. These results suggest that protein(s) present in the seminal plasma could interact with spermatozoal membranes and increase their fluidity.
D000177:Acrosome / Q000378:metabolism; D000818:Animals; D002118:Calcium / Q000378:metabolism; D002417:Cattle; D002462:Cell Membrane / Q000378:metabolism; D005456:Fluorescent Dyes; D066298:In Vitro Techniques; D008297:Male; D008560:Membrane Fluidity; D008561:Membrane Fusion; D008563:Membrane Lipids / Q000378:metabolism; D011485:Protein Binding; D011506:Proteins / Q000378:metabolism*; D029607:Seminal Vesicle Secretory Proteins; D013050:Spectrometry, Fluorescence; D013094:Spermatozoa / Q000378:metabolism*
D005456:Fluorescent Dyes; D008563:Membrane Lipids; D011506:Proteins; D029607:Seminal Vesicle Secretory Proteins; D002118:Calcium