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Proteases II pp 115-122 | Cite as

Human Bronchial Proteinase Inhibitor: Rapid Purification Procedure and Inhibition of Luecocyte Elastase in Presence and in Absence of Human Lung Elastin

  • C. Boudier
  • D. Carvallo
  • M. Bruch
  • C. Roitsch
  • M. Courtney
  • J. G. Bieth
Conference paper
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 240)

Abstract

Bronchial proteinase inhibitor (brl) is the most important inhibitor of human leucocyte elastase (HLE) present in upper airways secretions1. Its physiological function is probably to_ protect the bronchoalveolar tissues from HLE-induced proteolytic damage2,3 Published purification procedures of brl from bronchial sputum are based on Sepharose-bound chymotrypsin or trypsin, and yield an inhibitor preparation with a low specific activity and a multi-band pattern in SDS polyacrylamide gel electrophoresis4-6. In this paper we describe a purification procedure involving conventional chromatographic steps only and yielding a highly active inhibitor. The latter was used to study the kinetics of inhibition of HLE in a buffer system that mimics the physiological medium. Inhibition of HLE by brl was also investigated in presence of human lung elastin.

Keywords

Secretory Leukocyte Protease Inhibitor Bronchial Secretion Inhibition Curve Leukocyte Elastase Human Seminal Plasma 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1988

Authors and Affiliations

  • C. Boudier
    • 1
  • D. Carvallo
    • 2
  • M. Bruch
    • 1
  • C. Roitsch
    • 2
  • M. Courtney
    • 2
  • J. G. Bieth
    • 1
  1. 1.INSERM Unité 237Université Louis PasteurStrasbourgFrance
  2. 2.Transgène S.A. 11StrasbourgFrance

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