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3H-sialyl residues transfer by subcellular epididymal fractions [plasma membrane (PM), microsomes (MI), and mitochondria (MT)] to both endogenous and exogenous acceptors was studied. Their fraction purity was valued (5' nucleotidase and glucose 6-phosphatase activities). The glycoprotein or glycolipid N-acetyl neuraminyl transferase activity in microsomes were 5 times higher in caput than in cauda (624 to 125 pmoles/30 min/mg protein). PM activity also was higher in caput. In MT fraction, the activity was smaller. Two mechanisms related to spermatozoa glycoprotein changes during maturation are proposed: secretion to the lumen of molecules previously glycosilated in microsomes and transialylation to spermatozoa from membranal ectoenzymes localized on the surface of the epididymal epithelium.
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