TY - JOUR
T1 - Hemolysis and iodination of erythrocyte components by a myeloperoxidase mediated system
AU - Klebanoff, S. J.
AU - Clark, R. A.
PY - 1975
Y1 - 1975
N2 - Erythrocytes are hemolyzed by myeloperoxidase, an H2O2 generating system (glucose + glucose oxidase; hypoxanthine + xanthine oxidase) and an oxidizable cofactor (chloride, iodide, thyroxine, triiodothyronine). The combined effect of chloride and either iodide or the thyroid hormones is greater than additive. Myeloperoxidase can be replaced by lactoperoxidase in the iodide, thyroxine and triiodothyronine dependent, but not in the chloride dependent systems. Hemolysis is inhibited by the peroxidase inhibitors, azide and cyanide, and by catalase and is stimulated by superoxide dismutase when the xanthine oxidase system is employed as the source of H2O2. Hemolysis by the iodide dependent system is associated with the iodination of erythrocyte components.
AB - Erythrocytes are hemolyzed by myeloperoxidase, an H2O2 generating system (glucose + glucose oxidase; hypoxanthine + xanthine oxidase) and an oxidizable cofactor (chloride, iodide, thyroxine, triiodothyronine). The combined effect of chloride and either iodide or the thyroid hormones is greater than additive. Myeloperoxidase can be replaced by lactoperoxidase in the iodide, thyroxine and triiodothyronine dependent, but not in the chloride dependent systems. Hemolysis is inhibited by the peroxidase inhibitors, azide and cyanide, and by catalase and is stimulated by superoxide dismutase when the xanthine oxidase system is employed as the source of H2O2. Hemolysis by the iodide dependent system is associated with the iodination of erythrocyte components.
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U2 - 10.1182/blood.v45.5.699.699
DO - 10.1182/blood.v45.5.699.699
M3 - Article
C2 - 1173052
AN - SCOPUS:0016687587
SN - 0006-4971
VL - 45
SP - 699
EP - 707
JO - Blood
JF - Blood
IS - 5
ER -