Phospholipase and lysophospholipase activities of goat spermatozoa in transit from the caput to the cauda epididymidis.
Phospholipase and lysophospholipase activities were assayed in goat epididymal spermatozoa. Lysophospholipase was 10 times more active than phospholipase, and both enzymes decreased in activity substantially in the transit of spermatozoa from the caput to the cauda epididymidis. A comparative study revealed that phosphatidyl-ethanolamine, -choline and -inositol and phosphatidic acid were hydrolysed by goat sperm phospholipase. Hydrolysis of phosphatidylethanolamine/phosphatidylcholine revealed the end products to be glycerophosphoethanolamine/choline but neither diglycerides nor lysophosphatidylethanolamine/lysophosphatidylcholine were detected.
D000818:Animals; D004822:Epididymis / Q000502:physiology; D006041:Goats; D006868:Hydrolysis; D008245:Lysophospholipase / Q000378:metabolism; D008246:Lysophospholipids; D008297:Male; D010740:Phospholipases / Q000378:metabolism*; D010743:Phospholipids / Q000378:metabolism; D013083:Sperm Transport; D013094:Spermatozoa / Q000201:enzymology*
D008246:Lysophospholipids; D010743:Phospholipids; D010740:Phospholipases; D008245:Lysophospholipase