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PubMed1986

Red blood cell 2,3-diphosphoglyceric acid following ethanol consumption in man.

The red blood cell 2,3-diphosphoglycerate (DPG) concentration is reported in 33 ethanol abusers, 16 healthy ethanol users and 14 non-users. The results demonstrate an ethanol-associated increase in DPG content which returns to normal exponentially in the week following alcohol withdrawal. As well as implying a significant degree of hypoxia in association with quite moderate drinking, the fact that ethanol is not catabolized in red cells indicates that this effect is transmitted there, and hence to the rest of the organism, by some other agent. Carbon dioxide in subnormal quantities has the necessary characteristics.

Alcohol Drinking↗
PubMed1981

Effects of 2,3-diphosphoglyceric acid on the human erythrocyte membrane phosphorylation system.

The effect of 2,3-diphosphoglycerate (2,3-P2-glycerate) on the phosphorylation of spectrin in solution by purified membrane cyclic AMP-independent protein kinase and in membrane preparations by the endogenous kinase was investigated. 2,3-P2-Glycerate inhibited spectrin phosphorylation both in solution and in the intact membrane. Kinetic analyses showed that 2,3-P2-glycerate had no effect on the Km for ATP but appeared to lower the Vmax of the reaction. When the effect of 2,3-P2-glycerate was examined in the presence of varying concentrations of spectrin, competitive inhibition kinetics were obtained. Interestingly, low concentrations of 2,3-P2-glycerate were found to effect the release of the membrane kinase from erythrocyte membranes. This release reaction may be related to the ability of 2,3-P2-glycerate to interfere with the interaction between the kinase and spectrin. The data suggest the possibility that the kinase may be bound to spectrin in the erythrocyte membrane. 2,3-P2-glycerate also caused the solubilization of 3-phosphoglyceraldehyde dehydrogenase, but not of cyclic AMP-dependent protein kinase. Taken together, our data indicate that 2,3-P2-glycerate may have a regulatory role in membrane protein phosphorylation and also may regulate the extent of association of the kinase with the membrane.

2,3-Diphosphoglycerate↗