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. 1980 Jun 1;187(3):837–841. doi: 10.1042/bj1870837

Association of glyceraldehyde 3-phosphate dehydrogenase with the membrane of the intact human erythrocyte.

S Keokitichai, J M Wrigglesworth
PMCID: PMC1162469  PMID: 6821371

Abstract

Intact human erythrocytes were exposed to low concentrations of glutaraldehyde. After washing and subsequent lysis of the cells, glyceraldehyde 3-phosphate dehydrogenase activity is found to be associated with a membrane fraction and cannot be eluted by salt treatment. Lactate dehydrogenase activity is associated with a supernatant fraction under the same conditions. Preincubation of the intact cells under conditions designed to increase internal NADH concentrations, leads to a lower membrane-associated activity of glyceraldehyde 3-phosphate dehydrogenase after lysis.

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Selected References

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