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Ogawa, H, Kusumi, I, Ogata, A, Wada, A, Sakagami, H, Mitsuhashi, K and Date, K' (2015) Autoactivation of pancreatic trypsinogen is controlled by carbohydrate-specific interaction. FEBS Lett. '
Activation of bovine pancreatic trypsinogen (BPTG) by trypsin (BPT) was found to be inhibited by d GalN/GalNAc at pH 5.5, the pH of secretory granules in the pancreas. Binding studies with biotinylated sugar-polymers indicated that BPTG and BPT bind to α-GalNAc, α-Man, and α-Gal better at pH 5.5 than at pH 7.5. Ultraviolet-difference spectra indicated that BPTG binding to α-GalNAc differs substantially from BPTG binding to other sugars. The N-α-benzoyl-d,l-arginine-p-nitroanilide hydrochloride-hydrolyzing activity of BPT was only slightly affected by these sugars. The results indicate that the binding of GalNAc - containing glycoconjugates protects BPTG from autoactivation, and this may be a self-defense mechanism against intrapancreatic activation.
|Gene product||Qualifier||GO Term||Evidence Code||with/from||Aspect||Extension||Notes||Status|
|GO:0032023: trypsinogen activation||
Controlled by carbohdrate-specific interaction
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