Allosteric interactions governing oxygen equilibria in the haemoglobin system of the spiny dogfish, Squalus acanthias.
The oxygenation-linked, allosteric interactions of erythrocytic organic phosphates and urea with the haemoglobin (Hb), and the functional significance of the Hb multiplicity, were studies in an elasmobranch, Squalus acanthias. The autochthonous red cell nucleoside triphosphates (NTP) ATP and GTP (guanosine triphosphate) strongly depress O2 affinity of the stripped (cofactor-free) Hb and increase cooperativity in O2 binding. As previously found in teleost Hbs, GTP exerts a greater effect than ATP at the same concentration. Urea, in contrast, increases O2 affinity and depresses cooperativity. It also antagonizes the modulator effectivity of NTP at physiological NTP/Hb concentration ratios. Deoxygenation of the Hb raises blood pH. This Haldane effect contrasts with earlier findings for Pacific specimens, but accords with the presence of a Bohr effect (phi = delta log P50/delta pH). S. acanthias Hb resolves into six main components (three pairs) on the basis of isoelectric point. There is no evidence for radical functional differentiation as found in teleosts with electrophoretically anodal and cathodal Hb components. The physiological implications of the findings and the possible molecular mechanisms basic to the NTP and urea effects are discussed.
D000255:Adenosine Triphosphate / Q000097:blood; D000494:Allosteric Regulation; D000818:Animals; D001639:Bicarbonates / Q000097:blood; D002021:Buffers; D004284:Dogfish / Q000097:blood*; D006160:Guanosine Triphosphate / Q000097:blood; D006454:Hemoglobins / Q000502:physiology*; D006863:Hydrogen-Ion Concentration; D010100:Oxygen / Q000097:blood; D012754:Sharks / Q000097:blood*; D013696:Temperature; D014508:Urea
D001639:Bicarbonates; D002021:Buffers; D006454:Hemoglobins; D006160:Guanosine Triphosphate; D000255:Adenosine Triphosphate; D014508:Urea; D010100:Oxygen