NDLI: Hemolysis and iodination of erythrocyte components by a myeloperoxidase- mediated system

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Hemolysis and iodination of erythrocyte components by a myeloperoxidase- mediated system

Content Provider	Scilit
Author	Klebanoff, Sj Clark, Ra
Copyright Year	1975
Description	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 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.
Related Links	https://ashpublications.org/blood/article-pdf/45/5/699/578602/699.pdf
Ending Page	707
Page Count	9
Starting Page	699
DOI	10.1182/blood.v45.5.699.699
Journal	Blood
Issue Number	5
Volume Number	45
Language	English
Publisher	American Society of Hematology
Publisher Date	1975-05-01
Access Restriction	Open
Subject Keyword	Medical Laboratory Technology Myeloperoxidase Hemolysis Hormones Erythrocyte Azide Hypoxanthine H2o2 Iodide Lactoperoxidase Iodination Journal: Blood (Vol- 80, Issue- 5)
Content Type	Text
Resource Type	Article

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