Membrane protein cross-linking is an early step in the pathogenesis of copper-induced hemolytic anemia
- 31 December 1979
- journal article
- research article
- Published by Biomedical Research Press in Biomedical Research
- Vol. 1 (6) , 548-551
- https://doi.org/10.2220/biomedres.1.548
Abstract
Red cells [human] incubated with copper sulfate were tested for osmotic fragility, deformability and electrophoretic properties of membrane proteins. Cu treatment oxidized the SH of the membrane proteins to form intermolecular disulfide bonds, causing a reduction in membrane flexibility. Reduction in membrane flexibility was a major cause of the decreased red cell deformability in the early and mild toxic stages, before cell damage decreased the surface/vol ratio and increased the viscosity of red cell contents.This publication has 3 references indexed in Scilit:
- Evidence suggesting direct oxidation of human erythrocyte membrane sulfhydryls by copperBiochemical and Biophysical Research Communications, 1978
- Copper-Induced Acute Hemolytic AnemiaAnnals of Internal Medicine, 1970
- Hemolytic Anemia in Wilson's DiseaseAnnals of Internal Medicine, 1970