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Proteolytic inactivation of human leukocyte elastase

Experientia volume 41, pages 638–640 (1985)Cite this article

Summary

Human leukocyte elastase can be proteolytically inactivated by bovine pancreatic trypsin. Neither porcine pancreatic elastase nor bovine pancreatic chymotrypsin causes inactivation of leukocyte elastase, nor are trypsin, pancreatic elastase, or chymotrypsin themselves susceptible to proteolysis. The trypsin-catalyzed inactivation of leukocyte elastase can be slowed by inhibition of trypsin with benzamidine or by occupation of elastase's active site with elastatinal.

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Abbreviations

HLE:

human leukocyte elastase

PPE:

porcine pancreatic elastase

BPT:

bovine pancreatic trypsin β-trypsin

CT:

bovine pancreatic α-chymotrypsin

MeOSuc:

methoxysuccinyl

pNA:

p-nitroaniline

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Author information

Affiliations

  1. Pulmonary Pharmacology Section, Department of Biomedical Research, Stuart Pharmaceuticals, Division of ICI Americas Inc., 19897, Wilmington, Delaware, USA

    R. L. Stein & J. C. Williams

Authors
  1. R. L. Stein
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  2. J. C. Williams
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Stein, R.L., Williams, J.C. Proteolytic inactivation of human leukocyte elastase. Experientia 41, 638–640 (1985). https://doi.org/10.1007/BF02007697

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  • DOI: https://doi.org/10.1007/BF02007697

Key words

  • Elastase
  • inactivation
  • proteolytic