INTERACTION OF HEMOGLOBIN WITH IONS - QUANTITATIVE DESCRIPTION OF STATE OF MAGNESIUM, ADENOSINE 5'-TRIPHOSPHATE, 2,3-BISPHOSPHOGLYCERATE, AND HUMAN HEMOGLOBIN UNDER SIMULATED INTRACELLULAR CONDITIONS
INTERACTION OF HEMOGLOBIN WITH IONS - QUANTITATIVE DESCRIPTION OF STATE OF MAGNESIUM, ADENOSINE 5'-TRIPHOSPHATE, 2,3-BISPHOSPHOGLYCERATE, AND HUMAN HEMOGLOBIN UNDER SIMULATED INTRACELLULAR CONDITIONS
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DOI:
10.1111/j.1432-1033.1973.tb03091.x
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发表时间:
1973-01-01
期刊:
影响因子:
--
通讯作者:
RAPOPORT, SM
中科院分区:
文献类型:
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作者:
GERBER, G;BERGER, H;RAPOPORT, SM
The intracellular distribution of ATP, 2,3‐bisphosphoglycerate(P2‐glycerate) and Mg2+was calculated for the oxygenated and deoxygenated human erythrocyte for the normal range and that of pathophysiological variations based on the association constants of the relevant complexes.The data indicate that about 20% of ATP is bound both in the oxygenated and deoxygenated cells, while 39 and 73% ofP2‐glycerate is bound under these conditions. An increase of the free Mg2+concentration from 0.7 to 1.1 mM is produced by complete deoxygenation of haemoglobin.The calculations would indicate that during deoxygenation of haemoglobin the hexokinase reacts to the increased concentration of the activator Mg2+and the decline of the inhibitorP2‐glycerate with an elevation of its activity which corresponds to experimental data on intact erythrocytes.TheP2‐glycerate formation rate in deoxygenated cells is stimulated about 2.5 times in comparison to oxygenated cells as estimated from the free concentration ofP2‐glycerate and the kinetic constants of bisphosphoglycerate mutase.An assessment of the possible influence of other anions including bicarbonate shows that the distribution of the species of ATP,P2‐glycerate and Mg2+are changed by less than 20%.Together with the data presented in the accompanying paper, the results given here indicate that the constants and estimates are approximately valid for intracellular conditions.