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Autoactivation of Pancreatic Trypsinogen Is Controlled by Carbohydrate-Specific Interaction

Autoactivation of Pancreatic Trypsinogen Is Controlled by Carbohydrate-Specific Interaction

Haruko Ogawa, Izumi Kusumi, Aya Ogata, Arisa Wada, Hiromi Sakagami, Kana Mitsuhashi, Kimie Date

FEBS Lett. 2015 Feb 27;589(5):569-75.

PMID: 25637872

Abstract:

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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP64815801	N-Benzoyl-Val-Gly-Arg p-nitroanilide hydrochloride		64815-80-1	Price

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