Literature DB >> 2465784

Kinetics of the inhibition of free and elastin-bound human pancreatic elastase by alpha 1-proteinase inhibitor and alpha 2-macroglobulin.

P Laurent1, J G Bieth.   

Abstract

At pH 8.0 and 25 degrees C alpha 1-proteinase inhibitor and alpha 2-macroglobulin bind human pancreatic elastase with rate constants of 4.7.10(5) M-1.s-1 and 6.4.10(6) M-1.s-1, respectively. The corresponding delay times of elastase inhibition in plasma are 0.4 s and 0.2 s, respectively, indicating that both inhibitors may act as physiological antielastases. Elastin impairs the elastase inhibitory capacity of alpha 1-proteinase inhibitor and alpha 2-macroglobulin. In presence of human elastin, the former behaves like a slow-binding elastase inhibitor, with a rate constant of about 260 M-1.s-1. In contrast, alpha 2-macroglobulin is a fast-binding inhibitor of elastin-bound elastase, but only one of its two sites is functioning in presence of elastin.

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Year:  1989        PMID: 2465784     DOI: 10.1016/0167-4838(89)90306-3

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  3 in total

1.  Pseudomonas aeruginosa elastase does not inactivate alpha 1-proteinase inhibitor in the presence of leukocyte elastase.

Authors:  M Padrines; J G Bieth
Journal:  Infect Immun       Date:  1989-12       Impact factor: 3.441

2.  Kinetics of the inhibition of human pancreatic elastase by recombinant eglin c. Influence of elastin.

Authors:  B Faller; S Dirrig; M Rabaud; J G Bieth
Journal:  Biochem J       Date:  1990-09-15       Impact factor: 3.857

3.  Soluble fibrin preparations inhibit the reaction of plasmin with alpha 2-macroglobulin. Comparison with alpha 2-antiplasmin and leupeptin.

Authors:  P K Anonick; S L Gonias
Journal:  Biochem J       Date:  1991-04-01       Impact factor: 3.857

  3 in total

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