We have measured the partial pressure of O2 at 50% saturation (P50) and the concentration of various phosphate compounds in the erythrocytes of the bar-headed goose and the guanaco to establish the cause of the high blood O2 affinity in animals who normally reside at high altitude. The same data were obtained in the blood of two goose species, that live at sea level, and in human blood. At standard conditions (pH 7.4, PCO2 40 Torr, 37 degrees C), P50 was 29.7 Torr in the blood of the bar-headed goose and was about 10 Torr higher in the goose species living at sea level. Since the concentration of organic phosphates was not markedly different in the erythrocytes of either goose species we conclude that the hemoglobin of the bar-headed goose reacts more weakly with organic phosphates, which can also be inferred from studies on purified hemoglobin solutions. Likewise, the low P50 of guanaco blood in comparison with human blood can be explained by a reduced interaction of 2,3-bisphosphoglycerate of guanaco hemoglobin compared to the human pigment.
Hypoxia is the stimulus for activation of red cell carbonic anhydrase II (CAII) and 2,3-diphosphoglycerate (2,3-DPG) synthesis of chick red blood cells during late embryonic development. We have tested whether plasma catecholamines are involved as hormonal mediators, because hypoxia is a well-known stimulus for catecholamine release in mammalian fetuses. Plasma catecholamines were measured in 8- to 16-day-old chick embryos. Plasma levels of norepinephrine (NE) were initially low, but its concentration increased rapidly from 2.7 nM (day 12) to 13.4 nM at day 13 and 25.5 nM at day 16. Epinephrine (E) was not detectable before day 13. Short-term hypoxic exposure of day 11 embryos (1-h incubation at 13.5% O2) increased plasma NE concentration fivefold compared with the controls but had no effect on E. During 15-h in vitro incubation of red blood cells from day 11, addition of 1 microM NE to the incubation medium increased the red cell 2,3-DPG concentration nearly threefold and CAII activity sixfold compared with the control. The CAII activity and 2,3-DPG concentration were also increased when cells were incubated with plasma from late chick embryos. The activation was induced by beta-adrenergic stimulation of adenylyl cyclase. Atenolol and propranolol blocked the effects of NE and embryonic chick plasma. Analysis of de novo protein synthesis ([35S]methionine incorporation) demonstrated that catecholamines stimulate the synthesis of several proteins besides CAII. The results indicate that developmental changes of plasma NE concentration are instrumental in the adenosine 3',5'-cyclic monophosphate-dependent activation of CAII and 2,3-DPG synthesis of red blood cells from late chick embryos.
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