Glycosidases are present on the surface of Drosophila melanogaster spermatozoa.
We investigated the presence of enzymes on the surface of Drosophila melanogaster spermatozoa that might bind the carbohydrate residues of the egg shell. Spectrophotometric and fluorimetric studies were used on whole spermatozoa to assay galactosyltransferase and glycosidase activities. No galactosyltransferase is present on the sperm surface, whereas two glycosidases, beta-N-acetylglucosaminidase (GlcNAc'ase) and alpha-mannosidase (Man'ase), have been evidenced. They have an optimal pH of 6-6.5 and 4, respectively. The same glycosidases were detected as soluble forms probably secreted by the seminal vesicle epithelium. We suggest that these enzymes might be involved in the recognition of alpha-mannose and beta-N-acetylglucosamine residues present on the egg shell at the site of sperm entry.
Cattaneo
F
F
Department of General Physiology and Biochemistry, University of Milan, Italy.
Pasini
M E
ME
Perotti
M E
ME
D000118:Acetylglucosaminidase / Q000378:metabolism; D000818:Animals; D002462:Cell Membrane / Q000201:enzymology; D004331:Drosophila melanogaster; D005260:Female; D005700:Galactosyltransferases / Q000378:metabolism; D006026:Glycoside Hydrolases / Q000378:metabolism*; D008297:Male; D008361:Mannosidases / Q000378:metabolism; D013084:Sperm-Ovum Interactions; D013094:Spermatozoa / Q000201:enzymology*; D013499:Surface Properties; D043323:alpha-Mannosidase
D005700:Galactosyltransferases; D006026:Glycoside Hydrolases; D008361:Mannosidases; D043323:alpha-Mannosidase; D000118:Acetylglucosaminidase