Black J A, Acott K M, Bufton L
Biochim Biophys Acta. 1985 Nov 27;810(2):246-51. doi: 10.1016/0005-2728(85)90139-2.
The storage lesion which limits the shelf life of human blood in blood banking is associated with a metabolic loss of 2,3-diphosphoglycerate and ATP. This metabolic loss is driven by intracellular ATPase which are usually considered to include the ion pumps and the reactions which maintain the discoid shape of the human erythrocyte. Under the acidic conditions of blood storage, the energy-yielding reactions of the glycolytic pathway are restricted at the hexokinase and phosphofructokinase steps. We show here that under such circumstances the enzyme of the diphosphoglycerate shunt, diphosphoglycerate mutase/phosphatase and the glycolytic enzyme phosphoglycerate kinase can form a futile cycle with ATPase activity. This ATPase activity responds to 2-phosphoglycolate which is known to activate both diphosphoglycerate mutase and diphosphoglycerate phosphatase reactions. When the enzymes of the futile cycle are combined with the enzymes of the lower glycolytic pathway in a reconstitution experiment designed to represent conditions within the stored erythrocyte, the futile cycle does provide an ATPase activity which results in the metabolic loss of 2,3-diphosphoglycerate. An isotope incorporation experiment demonstrates that the futile cycle is active in glucose-depleted erythrocytes.
血库中限制人血保质期的储存损伤与2,3 - 二磷酸甘油酸和ATP的代谢损失有关。这种代谢损失由细胞内ATP酶驱动，这些酶通常被认为包括离子泵以及维持人红细胞盘状形状的反应。在血液储存的酸性条件下，糖酵解途径的产能反应在己糖激酶和磷酸果糖激酶步骤受到限制。我们在此表明，在这种情况下，二磷酸甘油酸支路的酶、二磷酸甘油酸变位酶/磷酸酶和糖酵解酶磷酸甘油酸激酶可与ATP酶活性形成无效循环。这种ATP酶活性对2 - 磷酸乙醇酸有反应，已知2 - 磷酸乙醇酸可激活二磷酸甘油酸变位酶和二磷酸甘油酸磷酸酶反应。在旨在模拟储存红细胞内条件的重组实验中，当无效循环的酶与糖酵解下游途径的酶结合时，无效循环确实提供了一种ATP酶活性，导致2,3 - 二磷酸甘油酸的代谢损失。同位素掺入实验表明，无效循环在葡萄糖耗尽的红细胞中具有活性。
