Aug 1, 1976

Factors in the evolution of hemoglobin function

Federation Proceedings
A Riggs

Abstract

The packaging of vertebrate blood hemoglobins within cells places subtle constraints on hemoglobin evolution. Since the concentration of hemoglobin is near the solubility limit a selective advantage should exist for a noncomplementary external topology of amino acid residues. Further, any change in charge on the protein should alter ion distribution across the cell membrane and so modify ion-sensitive oxygen transport. An efficient hemoglobin must not only combine readily with oxygen at prevailing environmental oxygen pressures, but must also release it at metabolically appropriate pressures. These adaptations frequently employ different strategies to achieve the same objective in different animals. Some hemoglobins have evolved special properties unrelated to the transport of oxygen to metabolizing tissues. Thus many teleost fish have hemoglobins that discharge much of their oxygen at low pH even at high oxygen pressures. This property appears to aid in filling the swim bladder with oxygen. The hemoglobins of elasmobranchs have evoked a unique resistance to urea as a consequence of the high urea content of their blood. Sometimes the functional adaptations of hemoglobins are achieved by multiple hemoglobins in the same cells. O...Continue Reading

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Mentioned in this Paper

Vertebrates
Dioxygen
Teleost fish
Swim Bladder
Structure-Activity Relationship
Acclimatization
Elasmobranchii
Adaptation
Diphosphoglyceric Acids
Hemoglobin Measurement

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