Intact form of myeloperoxidase from normal human neutrophils
Myeloperoxidase (donor: H 2O 2 oxidoreductase, EC 1.11.1.7) of human polymorphonuclear neutrophils was purified rapidly in the presence of the protease inhibitors phenylmethanesulfonyl fluoride and pepstatin A. The purified enzyme behaved as a single molecular species in several nondenaturing electr...
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Veröffentlicht in: | Archives of biochemistry and biophysics 1982-03, Vol.214 (1), p.273-283 |
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Sprache: | eng |
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Zusammenfassung: | Myeloperoxidase (donor: H
2O
2 oxidoreductase, EC 1.11.1.7) of human polymorphonuclear neutrophils was purified rapidly in the presence of the protease inhibitors phenylmethanesulfonyl fluoride and pepstatin A. The purified enzyme behaved as a single molecular species in several nondenaturing electrophoretic and chromatographic systems. Peroxidase activity in fresh extracts of neutrophils from 20 normal persons and from 5 patients with polycythemia was electrophoretically identical to purified enzyme. Treatment with trypsin converted myeloperoxidase to multiple electrophoretic forms of active enzyme. Size (
M
r ca. 15,000 and ca. 55,000) and stoichiometry of the subunits of purified enzyme, and enzyme
M
r ca. 140,000, were compatible with intact myeloperoxidase having an
α
2
β
2 structure. We found no evidence for electrophoretically detectable genetic polymorphism of myeloperoxidase. Proteolytic degradation of myeloperoxidase probably accounted for electrophoretic heterogeneity of enzyme and for some constituent peptides described previously. |
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ISSN: | 0003-9861 1096-0384 |
DOI: | 10.1016/0003-9861(82)90031-5 |