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Maier, K.L. ; Matejkova, E. ; Hinze, H. ; Leuschel, L. ; Weber, H.P. ; Beck-Speier, I.

Different selectivities of oxidants during oxidation of methionine residues in the α-1-proteinase inhibitor.

FEBS Lett. 250, 221-226 (1989)
DOI PMC
Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
Oxidation of the reactive site methionine (Met) in α-1-proteinase inhibitor (α-1-PI) to methionine sulfoxide (Met(O)) is known to cause depletion of its elastase inhibitory activity. To estimate the selectivity of different oxidants in converting Met to Met(O) in α-1-PI, we measured the molar ratio Met(O)/α-1-PI at total inactivation. This ratio was determined to be 1.2 for both the myeloperoxidase/H2O2/chloride system and the related compound NH2Cl. With taurine monochloramine, another myeloperoxidase-related oxidant, 1.05 mol Met(O) were generated per mol α-1-PI during inactivation. These oxidants attack preferentially one Met residue in α-1-PI, which is identical with Met 358, as concluded from the parallelism of loss of elastase inhibitory activity and oxidation of Met. A similar high specificity for Met oxidation was determined for the xanthine oxidase-derived oxidants. In contrast, the ratio found for ozone and m-chloroperoxybenzoic acid was 6.0 and 5.0, respectively, indicating oxidation of additional Met residues besides the reactive site Met in α-1-PI, i.e. unselective action of these oxidants. Further studies were performed on the efficiency of oxidants for total depletion of the elastase inhibitory capacity of α-1-PI. Ozone and m-chloroperoxybenzoic acid were 10-fold less effective and the superoxide anion/hydroxyl radicals were 30-50-fold less effective to inactivate the elastase inhibitory activity as compared to the myeloperoxidase-derived oxidants. The myeloperoxidase-related oxidants are discussed as important regulators of α-1-PI activity in vivo.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Korrespondenzautor
Schlagwörter Chloroperoxybenzoic Acid, M- ; Methionine ; Methionine Sulfoxide ; Myeloperoxidase ; Ozone ; Proteinase Inhibitor, α-1- ; Sulfite ; Xanthine Oxidase
ISSN (print) / ISBN 0014-5793
e-ISSN 1873-3468
Zeitschrift FEBS Letters
Quellenangaben Band: 250, Heft: 2, Seiten: 221-226 Artikelnummer: , Supplement: ,
Verlag Elsevier
Nichtpatentliteratur Publikationen
Begutachtungsstatus Peer reviewed
Institut(e) Institut für Inhalationsbiologie