Involvement of cytochrome b-245 in the respiratory burst of human neutrophils
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چکیده
منابع مشابه
Phosphorylation of the subunits of cytochrome b-245 upon triggering of the respiratory burst of human neutrophils and macrophages.
Cytochrome b-245, the only clearly identified component of the microbicidal oxidase system of phagocytes, is a heterodimer consisting of a 23 kDa (alpha) and a 76-92 kDa (beta) subunit. This study was conducted to examine whether, in common with a number of proteins, the subunits of the cytochrome were phosphorylated upon activation of the oxidase. Both subunits were phosphorylated after activa...
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Room temperature, CO-difference spectra of intact rat polymorphonuclear leucocytes (neutrophils) revealed the presence of a number of CO-binding haemoproteins. Absorption maxima at 413, 540 and 570 nm were attributed to the CO-complex of cytochrome b-245 whereas an absorption maximum at 595 nm was assigned to the contribution from a myeloperoxidase complex, since an identical absorption maximum...
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Cytochrome b-245, the putative terminal component of the specialized cidal oxidase system of phagocytes, was measured in human monocytes in culture. There was a dramatic synthesis of the cytochrome, which increased by 27.3 +/- 2.0 pmol/day per 10(7) cells. This represents an increase of about 40%/day in the early stages and an overall 7-fold increase after 16 days. The protein content increased...
متن کاملRole of myeloperoxidase in the respiratory burst of human neutrophils.
Myeloperoxidase (MPO), a heme enzyme present in the primary granules of polymorphonuclear leukocytes (PMNs), has been demonstrated to participate in the oxygen-dependent microbicidal activity of these cells. Evidence for the importance of MPO in this role comes in part from studies of normal PMNs treated with the heme enzyme inhibitor, sodium azide. MPO has also been suggested to regulate the r...
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ژورنال
عنوان ژورنال: Infection and Immunity
سال: 1982
ISSN: 0019-9567,1098-5522
DOI: 10.1128/iai.38.3.1301-1303.1982