A zinc-dependent peptidase in prostatic organelles present in seminal plasma.
The electrophoretic seminal plasma protein pattern changes obviously within a few hours if the plasma is not frozen after the ejaculation. Mainly cathodal proteins disappear. Addition of serine protease inhibitors has no apparent affect, but o-phenanthroline markedly retards the conversions seen on electrophoresis. The subcellular organelles in seminal plasma are shown to contain a zinc ion dependent peptidase with optimal activity at pH 7.8. Estimations of enzyme activity may be performed using the elastase substrates n-tert butyloxycarbonyl-L-alanine-paranitrophenylester (Boc(Ala)) and succinyl(alanine)3-paranitroanilide (Suc(Ala)3pNA). The enzyme is inactivated by addition of o-phenanthroline and is completely reactivated by the addition of zinc ions.
D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004587:Electrophoresis, Agar Gel; D006801:Humans; D008297:Male; D009842:Oligopeptides / Q000378:metabolism; D009940:Organoids / Q000201:enzymology*; D010447:Peptide Hydrolases / Q000378:metabolism*; D010618:Phenanthrolines / Q000494:pharmacology; D011467:Prostate / Q000648:ultrastructure*; D011480:Protease Inhibitors / Q000494:pharmacology; D012661:Semen / Q000201:enzymology*; D015032:Zinc / Q000494:pharmacology*
D009842:Oligopeptides; D010618:Phenanthrolines; D011480:Protease Inhibitors; C015516:succinyl-trialanine-4-nitroanilide; D010447:Peptide Hydrolases; D015032:Zinc; C025205:1,10-phenanthroline