Abstract
This study demonstrates that alpha-mannosidase from rat epididymal fluid is a ligand for phosphomannosyl receptors on the sperm surface. This enzyme was bound to intact epididymal spermatozoa with high affinity and in saturable form, and the binding was inhibited by mannose-6-phosphate but not by phosphorylated derivatives of fructose. Treatment of the enzyme with sodium periodate inhibited the binding of alpha-mannosidase, confirming that a carbohydrate residue is involved in the interaction with spermatozoa. Evidence is also presented that the cation-independent phosphomannosyl receptors are responsible for the interaction with alpha-mannosidase. These findings suggest a new role for extracellular transport mediated by the mannose-6-phosphate receptor.
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