Effect of alpha 1-proteinase inhibitor and sulphated polysaccharides on the activity of m beta-acrosin.
Purified m beta-acrosin catalysed amidolysis in vitro of several p-nitroanilides with C-terminal arginine residues. alpha 1-proteinase inhibitor inhibited amidolysis catalysed by the enzyme. This effect of alpha 1-Proteinase inhibitor was not prevented by pre-incubation of the enzyme with heparin or any other glycosaminoglycan. Pre-incubation of the enzyme with sulphated dextran or sulphated cellulose alleviated the effect of alpha 1-proteinase inhibitor. These results are discussed in terms of possible in vivo modulation by alpha 1-proteinase inhibitor of acrosin activity.
D000176:Acrosin / Q000378:metabolism*; D000818:Animals; D001798:Blood Proteins / Q000494:pharmacology*; D010450:Endopeptidases / Q000378:metabolism*; D006025:Glycosaminoglycans / Q000494:pharmacology*; D006801:Humans; D007700:Kinetics; D008297:Male; D011134:Polysaccharides / Q000494:pharmacology*; D011480:Protease Inhibitors / Q000494:pharmacology*; D012756:Sheep; D013094:Spermatozoa / Q000201:enzymology; D013329:Structure-Activity Relationship; D000515:alpha 1-Antitrypsin
D001798:Blood Proteins; D006025:Glycosaminoglycans; D011134:Polysaccharides; D011480:Protease Inhibitors; D000515:alpha 1-Antitrypsin; D010450:Endopeptidases; D000176:Acrosin