Purification and properties of boar acrosin.
An isolation procedure in the presence of non-ionic detergents has been developed for the large-scale preparation of boar acrosin. Five steps including hydrophobic interaction chromatography on phenyl-Sepharose resulted in a 161-fold purification of the enzyme with an accumulation yield of 41%. The resultant acrosin preparation had a molecular weight of 38,000, an isoelectric point of 10.5 and a specific activity of 37 U/mg. Apparent homogeneity was judged by sodium dodecyl sulfate electrophoresis and isoelectric focusing. A polarity index of 41.2% was calculated from the amino acid composition. Acrosin was stable at pH 5.5 in the presence of 0.1% Triton X-100. In the absence of detergent acrosin was strongly adsorbed on plastic surfaces.
D000176:Acrosin / Q000302:isolation & purification*; D000327:Adsorption; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D010450:Endopeptidases / Q000302:isolation & purification*; D004789:Enzyme Activation; D008297:Male; D012661:Semen / Q000032:analysis; D013552:Swine / Q000378:metabolism*
D000596:Amino Acids; D010450:Endopeptidases; D000176:Acrosin