Changes in surface protein structure of bull spermatozoa during epididymal maturation.
The surface proteins of bull spermatozoa from caput and cauda epididymis were labelled by lactoperoxidase-catalyzed radioiodination and solubilized and analyzed by SDS-PAG-electrophoresis. The surface protein patterns of caput and cauda epididymal spermatozoa resembled each other but some distinct differences could be found. Caput epididymal spermatozoa revealed a protein peak with molecular weight of 15 000 - 18 000 daltons but this peak was not found on cauda epididymal spermatozoa. On caput epididymal spermatozoa the most intensely labelled protein peak was located between 90 000 and 100 000 daltons but on cauda epididymal spermatozoa the corresponding peak was only weakly labelled and had a molecular weight of 80 000 - 90 000 daltons. Surface protein with molecular weight of 42 000 - 47 000 daltons was dominating on cauda epididymal spermatozoa. The surface protein structure of cytoplasmic droplets did not drastically differ from that of epididymal spermatozoa.
D000818:Animals; D002417:Cattle; D004591:Electrophoresis, Polyacrylamide Gel; D004822:Epididymis / Q000254:growth & development*; D008297:Male; D008565:Membrane Proteins / Q000378:metabolism*; D008970:Molecular Weight; D013094:Spermatozoa / Q000254:growth & development* / Q000378:metabolism
D008565:Membrane Proteins