Results 301 to 310 of about 119,702 (326)
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Partial Myeloperoxidase Deficiency

Acta Haematologica, 1982
Neutrophil myeloperoxidase (MPO) activity was analyzed by a semi-quantitative cytochemical method in 268 subjects divided into several groups. 17 subjects with significantly reduced MPO activity were found: 11 of 23 in the preleukemia group, 2/14 AMLs, 1/20 myeloproliferative syndrome, 1/7 carcinoma with bone marrow metastases, 1/33 diabetes mellitus ...
P, Cech, P, Schneider, F, Bachmann
openaire   +2 more sources

Inhibition of Myeloperoxidase

2020
Myeloperoxidase participates in innate immune defense mechanism through formation of microbicidal reactive oxidants and diffusible radical species. A unique activity is its ability to use chloride as a cosubstrate with hydrogen peroxide to generate chlorinating oxidants such as hypochlorous acid, a potent antimicrobial agent.
Jala, Soubhye   +3 more
openaire   +2 more sources

Influence of myeloperoxidase-catalyzing reaction on the binding between myeloperoxidase and anti-myeloperoxidase antibodies

Human Immunology, 2012
In the current study, whether myeloperoxidase (MPO)-catalyzing reaction could influence the antigenicity of MPO was investigated. Hypochlorite acid, the main product of the catalytic reaction, could lower the binding between MPO-antineutrophil cytoplasmic antibodies (ANCA) and MPO when the available chlorine was higher than 0.031×10(-3) g/l.
Peng-Cheng, Xu   +4 more
openaire   +2 more sources

Endothelium, Myeloperoxidase, Anti-Myeloperoxidase Interaction in Vasculitis

1993
Antibodies to myeloperoxidase (MPO) are found in the sera of patients with microscopic polyarteritis and idiopathic crescentic glomerulonephritis. Their pathogenicity is unknown. Studies were carried out on the binding of MPO to cultured human umbilical vein endothelial cells and the recognition of endothelium-bound MPO by antibody to MPO.
M, Vargunam   +6 more
openaire   +3 more sources

[20] Human myeloperoxidase and hemi-myeloperoxidase

1986
Publisher Summary This chapter describes human myeloperoxidase (MPO) and hemi-MPO. MPO is an enzyme found in the azurophilic granules of mammalian neutrophils and is also identified in human monocytes. Its function is to kill bacteria that have been phagocytosed by these cells.
Patricia C. Andrews, Norman I. Krinsky
openaire   +1 more source

Myeloperoxidase

Analytical Biochemistry, 1968
Norman Felberg, Julius Schultz
openaire   +1 more source

MYELOPEROXIDASE*

Annals of the New York Academy of Sciences, 1958
openaire   +2 more sources

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