| Literature DB >> 6557666 |
J A Kramps, C van Twisk, A C van der Linden.
Abstract
L-Pyroglutamyl-L-prolyl-L-valine-p-nitroanilide was found to be a highly specific substrate for human granulocyte elastase. At pH 8.3 and 37 degrees C, its Km = 0.55 mmol/l and the value for kcat was 6 sec-1, whereas with porcine pancreatic elastase these values were approximately 2 mmol/l and less than 0.001 sec-1, respectively. It is not cleaved by trypsin or chymotrypsin. With granulocyte elastase this new substrate is 50 times more sensitive compared to succinyltrialanyl-p-nitroanilide. L-Pyroglutamyl-L-prolyl-L-valine-p-nitroanilide can also be used for the assay of granulocyte elastase inhibitors.Entities:
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Year: 1983 PMID: 6557666
Source DB: PubMed Journal: Scand J Clin Lab Invest ISSN: 0036-5513 Impact factor: 1.713