The Bohr effect, i.e. the pH dependence of the oxygen affinity of haemoglobins (Hbs) from a variety of vertebrates, and its modulation by temperature and other heterotropic effectors has been reviewed. Haemoglobins from vertebrates were not reviewed following the usual classification (i.e. mammals, birds, etc.); instead we have selected several key examples of animals, which are confronted with a similar environmental situation therefore displaying a similar life style. Hence, the paper starts from a description of the general concepts at the basis of the Bohr effect as exemplified by human HbA and goes towards the analysis of the modulation mechanisms which have been observed in different animals in response to the needs induced by: (i) life in cold environments; (ii) diving behaviour; (iii) flight; and (iv) aquatic life. The emerging picture indicates a complex organization of the information contained in the Hb molecule, the oxygen-binding properties of which depend both on the intrinsic characteristics of the protein and on its heterotropic interactions with ligands such as protons (Bohr effect), small anions like chloride and organic phosphates. In addition, each one of the functional effects induced by binding of a given effector appears to be under the strict control of temperature that enhances or decreases its relative weight with respect to all the others. It is just by this sophisticated network of interactions that the Hb molecule is able to satisfy the physiological requirements of a multitude of organisms without changing dramatically its quaternary structure.

Cartilaginous fish are very ancient organisms. In the Antarctic sea, the modern chondrichthyan genera are poorly represented, with only three species of sharks and eight species of skates; the paucity of chondrichthyans is probably an ecological consequence of unusual trophic or habitat conditions in the Southern Ocean. In the Arctic, there are 26 species belonging to the class Chondrichthyes. Fish in the two polar regions have been subjected to different regional histories that have influenced the development of diversity: Antarctic marine organisms are highly stenothermal, in response to stable water temperatures, whereas the Arctic communities are exposed to seasonal temperature variations. The structure and function of the oxygen-transport haem protein from the Antarctic skate Bathyraja eatonii and from the Arctic skate Raja hyperborea (both of the subclass Elasmobranchii, order Rajiformes, family Rajidae) is reported in the present paper. These species have a single major haemoglobin (Hb 1; over 80% of the total). The Bohr-proton and the organophosphate-binding sites are absent. Thus the haemoglobins of northern and southern polar skates appear functionally similar, whereas differences were observed with several temperate elasmobranchs. Such evidence suggests that, in temperate and polar habitats, physiological adaptations have evolved along distinct pathways, whereas, in this case, the effect of the differences characterizing the two polar environments is negligible.