Elastase-alpha 1 proteinase inhibitor assay.
نویسندگان
چکیده
منابع مشابه
Pseudomonas aeruginosa elastase does not inactivate alpha 1-proteinase inhibitor in the presence of leukocyte elastase.
Pseudomonas aeruginosa elastase rapidly inactivates alpha 1-proteinase inhibitor by splitting its Pro-357-Met-358 peptide bond. The present study was aimed at testing whether this reaction takes place in the presence of leukocyte elastase. To this end was added alpha 1-proteinase inhibitor to a mixture of the two elastases, and we performed the following assays: (i) measurement of the residual ...
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A solid phase, enzyme-linkcd immunoassay is described for the quantitative determination of the complex of human granulocyte elastase (EC 3.4.21.37) with αι-proteinase inhibitor. The assay employs antibody-coated test tubes and it is suitable for routine use in clinical chemistry laboratories. Data for sample stability and test characteristics are given. A reference r nge of 20—180 μg/l elastas...
متن کاملLocal increase of antiprotease and neutrophil elastase-alpha 1-proteinase inhibitor complexes in lung cancer.
Tumour progression is dependent on many factors including antiproteases and proteases released by tumour cells or host cells infiltrating the tumour. In the present study, we evaluated the antiprotease content, namely alpha 2-macroglobulin (A2M) and alpha 1-proteinase inhibitor (A1PI) and neutrophil (PMN) elastase complexed with A1PI, in limited and extended lung cancer patients compared to a n...
متن کاملLimited proteolysis by macrophage elastase inactivates human alpha 1- proteinase inhibitor
Inflammatory mouse peritoneal macrophages secrete a metalloproteinase that is not inhibited by alpha 1-proteinase inhibitor. This proteinase, macrophage elastase, recognizes alpha 1-proteinase inhibitor with macrophage elastase does not involve a stable proteinase-inhibitor complex and results in the proteolytic removal of a peptide of apparent molecular weight 4,000-5,000 from the inhibitor. A...
متن کاملInteraction of mouse macrophage elastase with native and oxidized human alpha 1-proteinase inhibitor.
Native and oxidized alpha 1-proteinase inhibitor (alpha 1-PI) were compared as substrates for the metalloproteinase macrophage elastase. At substrate concentrations at which native alpha 1-PI was readily degraded by macrophage elastase, oxidized alpha 1-PI was hardly degraded at all. Incubation of macrophage elastase with oxidized alpha 1-PI before the addition of native alpha 1-PI showed that ...
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ژورنال
عنوان ژورنال: Annals of the Rheumatic Diseases
سال: 1991
ISSN: 0003-4967
DOI: 10.1136/ard.50.2.133