pH dependence of salt activation of human leukocyte elastase

Archives of Biochemistry and Biophysics
G OshimaM Yamada

Abstract

The effects of pH on salt stimulation of the rates of hydrolysis of three substrates by human leukocyte elastase were studied. The enzyme was most active at pH 10.5, 8.0-8.5, and 9.5 for the hydrolyses of fluorescein isothiocyanate-labeled S-carboxymethylated bovine serum albumin (FITC-CM-BSA), succinyl-L-Ala-L-Pro-L-Ala-7-methylcoumaryl-4-amide (Suc-APA-MCA), and succinyl-L-Ala3-p-nitroanilide (Suc-Ala3-pNA), respectively, in the absence of NaCl. The enzyme was activated by 0.5 M NaCl similarly at all pHs tested for the hydrolysis of Suc-Ala3-pNA, but more at neutral and alkaline pH values, respectively, for the hydrolyses of FITC-CM-BSA and Suc-APA-MCA. Thus, in the presence of 0.5 M NaCl, the enzyme was most active at pH 8.0 and 10.0 with FITC-CM-BSA and Suc-APA-MCA, respectively. In contrast, the proteolytic activity of porcine pancreatic elastase was somewhat inhibited by 0.5 M NaCl.

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Citations

Feb 1, 1992·Biochimica Et Biophysica Acta·T Imamura, T Kambara
Jul 7, 2007·Scandinavian Journal of Gastroenterology·Tadashi KohnoKunihiko Shibata
Dec 28, 1999·Respirology : Official Journal of the Asian Pacific Society of Respirology·W IchikawaS Sone
Oct 14, 2018·The Journal of Biological Chemistry·Takushi FujimotoHiroshi Kadokura
Aug 1, 1990·Biological Chemistry Hoppe-Seyler·H R WenzelH Tschesche
Oct 1, 1991·Biological Chemistry Hoppe-Seyler·G Oshima, M Yamada
Sep 23, 1997·Biochemical and Biophysical Research Communications·K SudoT Yokota
May 15, 1990·Thrombosis Research·G Oshima

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