N-Acetyl-DL-phenylalanine β-naphthyl ester (NAPBNE), a chromogenic substrate, is used to identify, differentiate and characterize serine protease(s) and peptidase(s).
An improved, time efficient, visual assay for quantitative determination of proteinase inhibitor activity in protein extracts is reported. Proteinase inhibitor activity of mammalian, bacterial, and fungal serine proteinases can be quantified. The method relies on radial diffusion of proteinase inhibitor
Molecular & general genetics : MGG, 243(6), 674-680 (1994-06-15)
Mutations at the apeA locus in Salmonella typhimurium lead to loss of a soluble enzyme ("protease I") that hydrolyzes the chromogenic endoprotease substrate N-acetyl phenylalanine beta-naphthyl ester. We have isolated pseudorevertants of S. typhimurium apeA mutations that have regained the
Two cytochemical methods for detection of granulocytic elastase and chymotrypsin employing alanine and phenylalanine naphthyl esters were developed. Specificity of reaction with the ester substrates was proven by chloromethyl ketone inhibitors. The results of both staining methods were almost identical
A cationic Schistosoma mansoni cercarial antigen was shown to be a serine protease as it was capable of hydrolysing N-acetyl-DL-phenylalanine beta-naphthyl ester (NAPBNE) after precipitation by immunoelectrophoresis, and this reaction was modulated by the serine protease inhibitors phenylmethanesulfonyl fluoride (PMSF)
Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research, 22(8), 847-852 (2002-10-25)
This study investigates the possible involvement of serine proteases in interferon-gamma (IFN-gamma) activity on WISH cells. It was observed that inhibition of (3)H-thymidine incorporation induced by IFN-gamma was abrogated by the serine protease inhibitors Nalpha-tosyl-L-lysyl-chloromethane and soybean trypsin inhibitor, both
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