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  • Title: Postnatal regulation of 2,3-DPG in sheep erythrocytes.
    Author: Mueggler PA, Carpenter S, Black JA.
    Journal: Am J Physiol; 1983 Sep; 245(3):H506-12. PubMed ID: 6311032.
    Abstract:
    The erythrocyte 2,3-diphosphoglycerate (2,3-DPG) concentrations of sheep change markedly during the 1st mo following birth. From measurements of erythrocyte glycolytic enzymes and intermediate concentrations, we have identified the mechanism regulating erythrocyte 2,3-DPG in postnatal sheep. The postnatal changes in erythrocyte 2,3-DPG do not result from qualitative or quantitative changes in the intracellular activities of the Rapoport-Luebering shunt enzymes, 2,3-DPG mutase or 2,3-DPG phosphatase. The postnatal 2,3-DPG changes result from changes in the erythrocyte concentration of 1,3-DPG, which is controlled by other reactions in the glycolytic pathway. Neither changes in the glycolytic control enzymes (hexokinase, phosphofructokinase, and pyruvate kinase) nor changes in the intrinsic glycolytic rate can account for these 1,3-DPG concentration changes. 1,3-DPG concentrations are regulated by the in vivo glycolytic rate, which is controlled by the intracellular concentration of glucose, the glycolytic substrate. Glucose concentrations are 0.3 mmol/l cells in erythrocytes of fetal sheep (135-140 days gestational age), increase following birth to a peak of 3.8 mmol/l cells by the 1st wk of age, and then decline to the normal adult levels of 0.5 mmol/l cells by the end of the 1st mo.
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