zymogen

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Related to Zymogens: Isoenzymes, Isozymes

zymogen

[′zī·mə·jən]
(biochemistry)
The inactive precursor of an enzyme; liberates an active enzyme on reaction with an appropriate kinose. Also known as proenzyme.
References in periodicals archive ?
They confirmed experimentally in vivo and in vitro that decreasing pH (acidifying) increases the sensitivity of the acinar cells to zymogen activation.
1985) Multi plicity and intermediates of the activation mechanism of zymogens of gastric aspartic proteinases.
During in situ zymography these zymogens would remain separated from activating enzymes, as the tissue remains relatively intact using this method (Galis et al.
The latter may be caused by rendering the acinar cells more sensitive to the action of cholecystokinin, a physiological stimulus to zymogen secretion that in higher concentrations causes pancreatitis, making the acinar cells secrete their zymogens to the basolateral side [49, 50], rather than to the apical side, where they are normally secreted.
In brief, the mucosal proteolytic zymogens were activated by adjusting the mucosal supernatant to pH 2.
1985a), observed vesicles budding from Golgi bodies in the F-cells of fed green tiger prawn Penaeus semisulcatus and suggested that these vesicles were enzyme precursors or zymogens, but this is yet to be confirmed or observed in other penaeids (Dall 1992, Icely & Nott 1992).
Cellular events responsible for autoproteolytic matriptase activation include oligomerization of matriptase zymogens and hepatocyte growth factor activator inhibitor (HAI-1) and conversion of single-chain zymogen to two-chain active protease.
These zymogens can be cleaved to form active enzymes following the induction of apoptosis.
Inhibition spectra of the two human trypsins derived from their purified zymogens.
Secreted as zymogens (pro-MMPs), MMPs are activated by a variety of proteinases, and their activity is highly regulated by interaction with tissue inhibitors of metalloproteinase (TIMPs) and by [alpha]2-macroglobulin.
The pancreatic zymogens were activated with purified enterokinase (Sigma, 71K7665) using the procedure described by Glazer and Steer (1977) before determination of trypsin and protease.
These substances are main components of many poisonous spiders and are named "glutamate receptor antagonists" [10], rich in proteins with N-mannase residues (Loxolisine B) that provide the gelatinolytic activity, identified as two zymogens (serine-protease) of 85 and 95 KDa with no lamininolytic activity [99,108].