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In membranes associated with purified pancreatic zymogen granules, GTP[S] elicited a concentration-dependent activation of phospholipase A2 (PLA2), which was converted to inhibition in the presence of added Ca2+. The GTP-binding protein inhibitor GDP[S] blocked both the stimulatory and inhibitory actions of GTP[S]. We conclude that in zymogen granule membranes GTP-binding proteins exert a dual regulation of PLA2 activity.
PLA2, phospholipase A2; GTP[S], guanosine 5′-[γ-thio]triphosphate; GDP[S], guanosine 5′[β-thio]diphosphate; GTP, guanosine triphosphate
@heena oops! this is insufficient for me. can i get a better answer ?
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zymogen is an inactive proenzyme secreted by pancreas. it protects the proteins from getting digested in the cells in which it is secreted.
A zymogen (or proenzyme) is an inactive enzyme precursor. A zymogen requires a biochemical change (such as a hydrolysis reaction revealing the active site, or changing the configuration to reveal the active site) for it to become an active enzyme. The biochemical change usually occurs in a lysosome where a specific part of the precursor enzyme is cleaved in order to activate it. The amino acid chain that is released upon activation is called the activation peptide.
The pancreas secretes zymogens partly to prevent the enzymes from digesting proteins in the cells in which they are synthesised. Fungi also secrete digestive enzymes into the environment as zymogens. The external environment has a different pH than inside the fungal cell and this changes the zymogen's structure into an active enzyme.
aks42 is right. Lots of enzymes are produced in the zymogen form to stop them from damaging things before they get to the location where they are supposed to work. A simple change (usually removal of part of the protein) makes it active!