N-acetyl-(L-Ala)3-p-nitroanilide as a new chromogenic substrate for elastase

Gad Feinstein, Abraham Kupfer, Mordechai Sokolovsky

Research output: Contribution to journalArticle

Abstract

The introduction of a useful new chromogenic substrate for the determination of elastase (EC 3.4.4.7) activity is described. N-acetyl-L-Ala-L-Ala-L-Ala-p-nitroanilide (AcAla3NA) is a new specific elastase substrate whose hydrolysis can be followed spectrophotometrically at 410 nm in a wide pH range. Its rate of hydrolysis by α-chymotrypsin (EC 3.4.4.5) and trypsin (EC 3.4.4.4.) is 0.02% and 0.001% respectively compared to its rate of hydrolysis by elastase. As little as 0.1 μg elastase/ml can be satisfactorily determined. At pH 8, Km = 0.88 mM and kcat = 11.9 sec-1.

Original languageEnglish (US)
Pages (from-to)1020-1026
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume50
Issue number4
DOIs
StatePublished - Feb 20 1973

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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