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Oxygen binding by hemoglobin

The structural arguments advanced here to explain f oxygen binding by hemoglobin are supported by comparisons of the amino acid sequences of a and j8 chains for a large number of hemoglobins from different species. Data from 60 species of a chains and 66 species of )S chains... [Pg.108]

Figure J-12 Oxygen binding by hemoglobin in the absence and in the presence of COi. ... Figure J-12 Oxygen binding by hemoglobin in the absence and in the presence of COi. ...
We have already mentioned that disturbance of BPG metabolism can affect oxygen binding by hemoglobin. Figure 6.9 shows the effect on oxygen saturation curves. [Pg.179]

Oxygen binding by hemoglobin is an example of cooperativity. In a similar way,... [Pg.232]

See also Oxygen Binding by Myoglobin, Oxygen Binding by Hemoglobin, Models of Allosteric Activity, Histidine... [Pg.412]

Figure 7.19l Combined effects of CO2 and BPG on oxygen binding by hemoglobin. [Pg.1304]

Fig. 44.11. Agents that affect oxygen binding by hemoglobin. Binding of hydrogen ions, 2,3 bisphosphoglycerate, and carbon dioxide to hemoglobin decrease its affinity for oxygen. Fig. 44.11. Agents that affect oxygen binding by hemoglobin. Binding of hydrogen ions, 2,3 bisphosphoglycerate, and carbon dioxide to hemoglobin decrease its affinity for oxygen.
Fig. 44.13. Effect of on oxygen binding by hemoglobin (Hb). A. In the tissues, CO2 is released. In the red blood cell, this CO2 forms carbonic acid, which releases protons. The protons bind to Hb, causing it to release oxygen to the tissues. B. In the lungs, the reactions are reversed. O2 binds to protonated Hb, causing the release of protons. They bind to bicarbonate (HCO3 ), forming carbonic acid, which is cleaved to water and CO2, which is exhaled. Fig. 44.13. Effect of on oxygen binding by hemoglobin (Hb). A. In the tissues, CO2 is released. In the red blood cell, this CO2 forms carbonic acid, which releases protons. The protons bind to Hb, causing it to release oxygen to the tissues. B. In the lungs, the reactions are reversed. O2 binds to protonated Hb, causing the release of protons. They bind to bicarbonate (HCO3 ), forming carbonic acid, which is cleaved to water and CO2, which is exhaled.
Oxygen binding by hemoglobin is vifry sensitive to pH. and Ihis is one of the reasons why pH coniiol in the bloodslream and olhc issues is pariicularly importani... [Pg.16]

Eaton, W. A., Henry, E. R., Hofrichter, J., Mozzarelli, A. 1999. Is cooperative oxygen binding by hemoglobin really understood Nat. Struct. Biol. 6, 351-358. [Pg.358]

Is the Consilient Mechanism Relevant to Oxygen Binding by Hemoglobin ... [Pg.256]

Bohr effect The effect of pH on oxygen binding by hemoglobin, by which a decrease in pH causes a decrease in oxygen affinity. The effect promotes both the release of oxygen from hemoglobin in the tissues and the release of CO2 from the blood to the air in the lungs. [Pg.1115]

Svetina, S., 1973, Thermodynamical studies of cooperative oxygen binding by hemoglobin, m "Proc. VII. Internationales Symposium liber Strukture und Funktion der Erytrozyten", Anhand-lungen der Akademie der Wissenschaften der DDR, Berlin, p. 135. [Pg.306]

See other pages where Oxygen binding by hemoglobin is mentioned: [Pg.626]    [Pg.84]    [Pg.54]    [Pg.55]    [Pg.56]    [Pg.153]    [Pg.187]    [Pg.189]    [Pg.199]    [Pg.115]    [Pg.401]    [Pg.402]    [Pg.408]    [Pg.1319]    [Pg.1932]    [Pg.28]    [Pg.305]   


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