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Evidence suggesting direct oxidation of human erythrocyte membrane sulfhydryls by copper

Biochemical and Biophysical Research Communications 82(4): 1294-1299

Evidence suggesting direct oxidation of human erythrocyte membrane sulfhydryls by copper

Cupric ion may directly oxidize the sulfhydryls of human erythrocyte membrane proteins leading to the formation of disulfide links. When packed ghosts were incubated in cupric sulfate (0.3 to 0.7 mM) at pH 8 and electrophoresed on sodium dodecyl sulfate polyacrylamide gels in the absence of dithiothreitol bands 1, 2 (spectrin); 4.2 and 5 (actin) diminished in intensity concomitant with the appearance of high MW material. Band 3 moved to its dimeric position on the gel. Evidence that these crosslinks result from formation of new disulfide links due to direct Cu binding includes: reversal of crosslinking upon addition of dithiothreitol; and blockage of the effect of N-ethylmaleimide, EDTA and mercuric chloride. The effect of Cu was observed under N2, suggesting that it is not related to air oxidation. The crosslinking effect does not require high Cu concentrations if the ghost concentration is low. The possible implication of these results with regard to Cu-induced hemolytic anemias is briefly discussed.

Accession: 005411891

PMID: 697795

DOI: 10.1016/0006-291x(78)90328-5

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