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Alpha‐1‐antitrypsin P Lowell : a normally functioning variant present in low concentration
Author(s) -
Cook L.,
Burdon J.,
Brenton S.,
Janus E. D.,
Knight K.
Publication year - 1995
Publication title -
australian and new zealand journal of medicine
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.596
H-Index - 70
eISSN - 1445-5994
pISSN - 0004-8291
DOI - 10.1111/j.1445-5994.1995.tb02855.x
Subject(s) - elastase , alpha 1 antitrypsin deficiency , neutrophil elastase , alpha (finance) , pancreatic elastase , medicine , enzyme , phenotype , proteinase inhibitor , pi , microbiology and biotechnology , endocrinology , immunology , biochemistry , biology , gene , inflammation , surgery , construct validity , patient satisfaction
Background: Alpha‐1‐antitrypsin deficiency is associated with a high risk for the development of emphysema, particularly for phenotype Pi ZZ, which is both deficient and an abnormal inhibitor of the powerful proteolytic enzyme, human neutrophil elastase. The rare variant P Lowell is also expressed at abnormally low levels, but its anti‐elastase activity has not been described. Aim: To study the anti‐elastase activity of alpha‐1‐antitrypsin P Lowdl and compare it to the common M, S and Z proteins. Method: Alpha‐1‐antitrypsin from a female patient aged 75 years with the rare genotype P LoweU Null Bcllingham was studied for its ability to inhibit human neutrophil elastase in a time dependent manner. Results: P Lowe ii has near normal function as an inhibitor of human neutrophil elastase with an association rate constant of 7.4 X 10 6 M'V 1 at 25 °C, similar to that of M and S. Conclusion: Alpha‐1‐antitrypsin P L is associated with a severe deficiency of alpha‐1‐antitrypsin similar to Z, but unlike that protein it has near normal function as an anti‐elastase.