Zona pellucida-binding and fucose-binding of boar sperm acrosin is not correlated with proteolytic activity.
The major fucose-binding protein of 53 kDa was isolated from boar spermatozoa by mild detergent extraction and subsequent high-performance gel filtration and reversed-phase high-performance liquid chromatography. This protein has been identified as high-molecular-mass acrosin by N-terminal sequencing. Treatment of the isolated protein with diisopropyl fluorophosphate abolishes the enzymatic activity but not the zona pellucida- and fucose-binding properties. Mercaptolysis and S-pyridyl-ethylation of native two-chain acrosin followed by HPLC and SDS-PAGE revealed that the binding properties are located on the acrosin heavy chain.
Töpfer-Petersen
E
E
Dermatologische Klinik und Poliklinik, Universität München.
Henschen
A
A
D000176:Acrosin / Q000037:antagonists & inhibitors / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D005643:Fucose / Q000378:metabolism*; D066298:In Vitro Techniques; D007531:Isoflurophate / Q000494:pharmacology; D037102:Lectins / Q000302:isolation & purification / Q000378:metabolism*; D008297:Male; D010063:Ovum / Q000378:metabolism*; D011485:Protein Binding; D012697:Serine Endopeptidases / Q000378:metabolism*; D013084:Sperm-Ovum Interactions; D013094:Spermatozoa / Q000201:enzymology*; D013552:Swine; D015044:Zona Pellucida / Q000378:metabolism*
D037102:Lectins; C027112:fucose-binding lectin; D007531:Isoflurophate; D005643:Fucose; D012697:Serine Endopeptidases; D000176:Acrosin