Acrosin shows zona and fucose binding, novel properties for a serine proteinase.
The major fucose-binding protein of 53 kDa from boar spermatozoa was isolated to apparent homogeneity using a two-step procedure including high-performance gel filtration and reversed-phase chromatography. The N-terminal sequence of the protein revealed that it is identical with the sperm proteinase acrosin. By means of a solid-phase zona-binding assay based on the avidin-biotin system it was demonstrated that acrosin also interacts strongly with porcine zona pellucida. Thus, the acrosin molecule combines specific proteolytic activity with zona- and carbohydrate-affinity properties, i.e. previously unrecognized properties of a serine proteinase. It seems likely that this special affinity of acrosin directs the proteolytic activity to its structural target in the vivo situation.
D000176:Acrosin / Q000378:metabolism*; D000818:Animals; D005260:Female; D005643:Fucose / Q000378:metabolism*; D008297:Male; D010063:Ovum / Q000378:metabolism*; D011485:Protein Binding; D012697:Serine Endopeptidases / Q000378:metabolism*; D013094:Spermatozoa / Q000201:enzymology*; D013552:Swine; D015044:Zona Pellucida / Q000378:metabolism*
D005643:Fucose; D012697:Serine Endopeptidases; D000176:Acrosin