THE SHIFT TO THE LEFT

PEDIATRICS ◽  
1971 ◽  
Vol 48 (6) ◽  
pp. 853-856 ◽  
Author(s):  
Frank A. Oski ◽  
Maria Delivoria-Papadopoulos

For many years it appeared that physiologists, and physiologists alone, puzzled over the causes and significance of alterations in the position of the oxygen-hemoglobin equilibrium curve. The reports by Benesch and Benesch1 and Chanutin and Curnish2 in 1967, concerning the role of red cell organic phosphates in determining the affinity of hemoglobin for oxygen, have served to rekindle curiosity in this problem of oxygen transport and produced a common focus of clinical interest for neonatologists, hematologists, biochemists, and the now nearly forgotten physiologists. The oxygen-hemoglobin equilibrium curve of normal adult blood is depicted as the center curve in Figure 1.

2009 ◽  
Vol 5 (3) ◽  
pp. 191-210 ◽  
Author(s):  
Jiří Palek ◽  
Libuše Mirčevová ◽  
Václav Brabec ◽  
Brfzřich Friedmann ◽  
Alexej Májský

1991 ◽  
Vol 260 (4) ◽  
pp. R798-R803
Author(s):  
M. Riera ◽  
J. F. Fuster ◽  
L. Palacios

The effects of two different degrees of experimentally induced anemia and the consequent high percentage of circulating immature erythrocytes on oxygen affinity (pH 7.5 and 41 degrees C), erythrocyte organic phosphates, and Hb fractions have been studied in quail. Blood reticulocytes reached percentages of 24 and 69-87% in the first and second experiments, respectively. Variations in the phosphate levels found during the anemic process were related to the amount of circulating reticulocytes. The erythrocyte [ATP] (brackets indicate concentration) and [ATP]/[Hb] molar ratio increased with the release of reticulocytes and returned to control levels as they matured. The erythrocyte [inositol pentakisphosphate (InsP5)] decreased significantly when circulating reticulocytes showed their highest values, whereas there was hardly any effect on the [InsP5]/[Hb] molar ratio, which changed only slightly. Hb-O2 affinity also exhibited no statistical changes associated with acute anemia. These latter findings indicate that InsP5, at physiological concentrations, is the primary modulator of quail Hb function; the observed rise in [ATP] has no additional influence on Hb-O2 affinity. It is suggested that InsP5 tends to maintain the blood oxygen affinity in both mature erythrocytes and reticulocytes. The main compensatory response at blood level is a rapid bulk reticulocyte release from medulla.


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