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Vertebrate Hemoglobins

Rolf L. Ingermann

10.1002/cphy.cp130106

Source: Supplement 30: Handbook of Physiology, Comparative Physiology

Originally published: 1997

Published online: January 2011

Full Article on Wiley Online Library



Abstract

The sections in this article are:

1 Homotrophic and Heterotrophic Interactions
1.1 Carbon Dioxide and Protons
1.2 Organic Phosphates
1.3 Sensitivity to Bicarbonate
1.4 Chloride
1.5 Acclimation and Extraerythrocytic Factors Influencing Oxygen Affinity through Heterotrophic Interactions
2 Hemoglobin Structure
2.1 Agnatha
2.2 Hemoglobin Heterogeneity
2.3 Possible Physiological Significance of Hemoglobin Heterogeneity
2.4 Other Possible Roles for Hemoglobin Heterogeneity
2.5 Additional Bases of Apparent Hemoglobin Heterogeneity
2.6 Association of Tetramers
3 Functional Adaptations in Hemoglobins
3.1 Scaling
3.2 Changes in Hemoglobins during Ontogeny
3.3 Adaptation to Temperature
3.4 Adaptation to Hypoxia
3.5 Diving Animals
4 Functional Adaptations: Adaptations Restricted to Specific Vertebrate Groups
4.1 Urea Insensitivity
4.2 Root Effect Hemoglobins
5 Conclusion
Figure 1. Figure 1.

Cooperative binding of oxygen by hemoglobin in dog blood as a function of carbon dioxide tensions. Dashed lines are rectangular hyperbolas with P50 values of 4 and 20 mm Hg for comparison. The ordinate is the percentage of oxygen saturation. The effect of carbon dioxide is due to direct binding and formation of carbaminohemoglobin and to the rise in proton concentration generated when carbon dioxide is hydrated by carbonic anhydrase to form carbonic acid. Data represented by solid lines are from Bohr et al. 58; figure is taken from Edsall 178 with permission.
Figure 2. Figure 2.

Cooperative binding of oxygen to human whole blood and cofactor‐free hemoglobin in the presence of carbon dioxide (40 mm Hg) and/or 2,3‐DPG (1.2 moles per mole hemoglobin tetramer) at 37°C. Figure is taken from Kilmartin and Rossi‐Bernardi, Physiological Reviews 325 with permission.
Figure 3. Figure 3.

A: Hypothetical oxygen equilibrium curves for red cells from fetal, nonpregnant (NPF), and pregnant garter snakes (Thamnophis elegans). P50 values at 20°C are from reference 294. Hill coefficient is taken to be 2.3 for each curve, and, as an approximation, it is assumed to remain constant over this range of oxygen saturations. Figure is from reference 292. B: Intracellular concentration of nucleoside triphosphate (primarily ATP [49]) in red cells from pregnant (PF) and nonpregnant (NPF) females, males (M), and fetal T. elegans as a function of time of year. (Confidence intervals represent means ± 1 SD.) Figure has been modified from reference 294 with permission.
Figure 4. Figure 4.

Oxygen equilibrium curves of the two primary trout (Salmo irideus = Oncorhynchus mykiss) hemoglobins, Hb I and Hb IV, at different pH values. A: Hb I at pH 6.8 (•), 7.2 (▴), 7.6 (▪); A and B: Hb IV at pH 8.5 (□), 7.4 (▵), 7.1 (▿), 6.7 (▾), and 6.1 (X). Studies were conducted at 20°C. Plot B clearly shows Hb IV to be a Root effect hemoglobin: it does not become fully saturated with oxygen even at very high oxygen tensions and loses cooperativity at low pH values. This figure is taken from Giardina et al. 216 with permission. Qualitatively very similar results have been reported by Hashimoto et al. 254 for the two primary hemoglobin components of chum salmon (Oncorhynchus keta).
Figure 5. Figure 5.

Wastl and Leiner's 1931 568 Hill plot of duck blood at various temperatures. Shown is the log (Y/[1–Y]) and percent saturation vs. the log of oxygen tension for blood in the presence of 40 mm Hg carbon dioxide. (Y is the fractional saturation of the blood with oxygen.) The plot clearly shows that the Hill coefficient exceeds 4.0 at saturations above, but not below, about 60%. Figure is taken from Pflügers Archiv with permission of Springer‐Verlag, publishers.
Figure 6. Figure 6.

Comparison of blood and hemoglobin oxygen affinity as a function of body mass. Figure is taken from Riggs 481 with permission. See also Figure 9.
Figure 7. Figure 7.

Decline in levels of fetal hemoglobins after birth in humans, cattle, sheep, goats, and two monkeys (Macaca nemestrina and Macaca speciosa). Figure is taken from Wood, News in Physiological Science 626 with permission.
Figure 8. Figure 8.

Effect of temperature on cofactor‐free human hemoglobin and hemoglobin from several fishes, including tuna (Thunnus). Remarkable is the relative temperature‐insensitivity of tuna hemoglobin. Figure is taken from Johansen and Lenfant 317.
Figure 9. Figure 9.

Summary comparison of blood oxygen affinity and body mass for diving and terrestrial mammals. Open circles indicate terrestrial mammals and filled circles indicate diving mammals. Each point represents P50 for a single species except, for points connected by a vertical line. In the latter case, P50 values represent the same species from different studies. Continuous line is a least squares regression of the values from terrestrial mammals only. Figure is taken from Snyder 514 with permission from Elsevier Science Publishers.


Figure 1.

Cooperative binding of oxygen by hemoglobin in dog blood as a function of carbon dioxide tensions. Dashed lines are rectangular hyperbolas with P50 values of 4 and 20 mm Hg for comparison. The ordinate is the percentage of oxygen saturation. The effect of carbon dioxide is due to direct binding and formation of carbaminohemoglobin and to the rise in proton concentration generated when carbon dioxide is hydrated by carbonic anhydrase to form carbonic acid. Data represented by solid lines are from Bohr et al. 58; figure is taken from Edsall 178 with permission.



Figure 2.

Cooperative binding of oxygen to human whole blood and cofactor‐free hemoglobin in the presence of carbon dioxide (40 mm Hg) and/or 2,3‐DPG (1.2 moles per mole hemoglobin tetramer) at 37°C. Figure is taken from Kilmartin and Rossi‐Bernardi, Physiological Reviews 325 with permission.



Figure 3.

A: Hypothetical oxygen equilibrium curves for red cells from fetal, nonpregnant (NPF), and pregnant garter snakes (Thamnophis elegans). P50 values at 20°C are from reference 294. Hill coefficient is taken to be 2.3 for each curve, and, as an approximation, it is assumed to remain constant over this range of oxygen saturations. Figure is from reference 292. B: Intracellular concentration of nucleoside triphosphate (primarily ATP [49]) in red cells from pregnant (PF) and nonpregnant (NPF) females, males (M), and fetal T. elegans as a function of time of year. (Confidence intervals represent means ± 1 SD.) Figure has been modified from reference 294 with permission.



Figure 4.

Oxygen equilibrium curves of the two primary trout (Salmo irideus = Oncorhynchus mykiss) hemoglobins, Hb I and Hb IV, at different pH values. A: Hb I at pH 6.8 (•), 7.2 (▴), 7.6 (▪); A and B: Hb IV at pH 8.5 (□), 7.4 (▵), 7.1 (▿), 6.7 (▾), and 6.1 (X). Studies were conducted at 20°C. Plot B clearly shows Hb IV to be a Root effect hemoglobin: it does not become fully saturated with oxygen even at very high oxygen tensions and loses cooperativity at low pH values. This figure is taken from Giardina et al. 216 with permission. Qualitatively very similar results have been reported by Hashimoto et al. 254 for the two primary hemoglobin components of chum salmon (Oncorhynchus keta).



Figure 5.

Wastl and Leiner's 1931 568 Hill plot of duck blood at various temperatures. Shown is the log (Y/[1–Y]) and percent saturation vs. the log of oxygen tension for blood in the presence of 40 mm Hg carbon dioxide. (Y is the fractional saturation of the blood with oxygen.) The plot clearly shows that the Hill coefficient exceeds 4.0 at saturations above, but not below, about 60%. Figure is taken from Pflügers Archiv with permission of Springer‐Verlag, publishers.



Figure 6.

Comparison of blood and hemoglobin oxygen affinity as a function of body mass. Figure is taken from Riggs 481 with permission. See also Figure 9.



Figure 7.

Decline in levels of fetal hemoglobins after birth in humans, cattle, sheep, goats, and two monkeys (Macaca nemestrina and Macaca speciosa). Figure is taken from Wood, News in Physiological Science 626 with permission.



Figure 8.

Effect of temperature on cofactor‐free human hemoglobin and hemoglobin from several fishes, including tuna (Thunnus). Remarkable is the relative temperature‐insensitivity of tuna hemoglobin. Figure is taken from Johansen and Lenfant 317.



Figure 9.

Summary comparison of blood oxygen affinity and body mass for diving and terrestrial mammals. Open circles indicate terrestrial mammals and filled circles indicate diving mammals. Each point represents P50 for a single species except, for points connected by a vertical line. In the latter case, P50 values represent the same species from different studies. Continuous line is a least squares regression of the values from terrestrial mammals only. Figure is taken from Snyder 514 with permission from Elsevier Science Publishers.

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Article Title: Vertebrate Hemoglobins
 

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Rolf L. Ingermann. Vertebrate Hemoglobins. Compr Physiol 2011, Supplement 30: Handbook of Physiology, Comparative Physiology: 357-408. First published in print 1997. doi: 10.1002/cphy.cp130106