The Action of Trypsin on Synthetic Chromogenic Arginine Substrates
- 1 January 1979
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 85 (1) , 157-162
- https://doi.org/10.1093/oxfordjournals.jbchem.a132305
Abstract
A new arginine derivative, N-benzyloxycarbonyl-L-phenylalanyl-L-valyl-L-arginine-p-nitroanilide hydrochloride (ZPVAPA.HCI) was synthesized by the condensation of N-benzyloxy-carbonyl-L-phenylalanyl-L-valine and L-arginine-p-nitroanilide dihydrochioride using dicyclohexylcarbodiimide as a coupling reagent and 1-hydroxy-benzotriazole as an additive. L-ZPVAPA.HCI was split by trypsin more readily than Na-benzyloxycarbonyl-L-arginine-p nitroanilide hydrochloride (L-ZAPA.HCI), Na-tosyl-L-arginine-p-nittroanilide hydrochloride (L-BAPA.HCI), N hydrochloride (L-TAPA.HCI) and Na-benzoyl-DL-arginine-p-nitroanilide hydrochloride (DL-BAPA.HCI) by factors of 100, 400, 600, and 1,200, respectively. Low concentrations of dimethyl formamide (DMF) enhanced the trypsin-catalyzed hydrolyses of L-ZAPA.HCI and L-TAPA.HCI, contrary to the findings of other authors that DMF has no effect on the tryptic hydrolysis.This publication has 0 references indexed in Scilit: