The Journal of Biochemistry
Online ISSN : 1756-2651
Print ISSN : 0021-924X
The Action of Trypsin on Synthetic Chromogenic Arginine Substrates
Oyin SOMORINSeiichi TOKURANorio NISHIJunzo NOGUCHI
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1979 年 85 巻 1 号 p. 157-162

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A new arginine derivative, N-benzyloxycarbonyl-L-phenylalanyl-L-valyl-L-arginine p-nitro-anilide hydrochloride (ZPVAPA. HCl) was synthesized by the condensation of N-benzyloxy-carbonyl-L-phenylalanyl-L-valine and L-arginine-p-nitroanilide dihydrochloride using dicyclo-hexylcarbodiimide as a coupling reagent and 1-hydroxy-benzotriazole as an additive. L-ZPVAPA.HCI was split by trypsin more readily than Nα-benzyloxycarbonyl-L-arginine p-nitroanilide hydrochloride (L-ZAPA. HCl), Nα-benzoyl-L-arginine p-nitroanilide hydrochlo-ride (L-BAPA. HCl), Nα-tosyl-L-arginine p-nitroanilide hydrochloride (L-TAPA. HCI) and Nα-benzoyl-DL-arginine p-nitroanilide hydrochloride (DL-BAPA. HCl) by factors of 100, 400, 600, and 1, 200, respectively. Low concentrations of dimethyl formamide (DMF) enhanced the trypsin-catalyzed hydrolyses of L-ZAPA. HCl and L-TAPA. HCl, contrary to the findings of other authors that DMF has no effect on the tryptic hydrolysis.
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© The Japanese Biochemical Society
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