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Isolation, properties, and complete amino acid sequence of human secretory leukocyte protease inhibitor, a potent inhibitor of leukocyte elastase.

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Thompson, R C, Ohlsson, K·1986·Proceedings of the National Academy of Sciences

Abstract

A potent inhibitor of human leukocyte elastase (EC 3.4.21.37) and cathepsin G (EC 3.4.21.20) and of human trypsin (EC 3.4.21.4) has been purified from human parotid secretions. The complete amino acid sequence of this protein has been determined. The sequence suggests that the protein has two domains of about 54 amino acids, each of which contains four disulfide bonds. On the basis of a limited homology to other protease inhibitors, the antielastase and antitrypsin activities are thought to be properties of the C-terminal and N-terminal domains, respectively. The affinity of the inhibitor for leukocyte elastase is very high, suggesting a functional role for the protein in preventing elastase-mediated damage to oral and possibly other mucosal tissues.

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Metadata

Authors
Thompson, R. C., & Ohlsson, K.
Venue
Proceedings of the National Academy of Sciences
Published
1986-09
Volume
83
Issue
18
Pages
6692-6696
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2024882709
Cited by
475
References
0
FWCI
3.38
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Isolation, properties, and complete amino acid sequence of human secretory leukocyte protease inhibitor, a potent inhibitor of leukocyte elastase. https://app.cochat.ai/papers/10.1073/pnas.83.18.6692
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Thompson, R. C., & Ohlsson, K. (1986). Isolation, properties, and complete amino acid sequence of human secretory leukocyte protease inhibitor, a potent inhibitor of leukocyte elastase. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.83.18.6692

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.