Functional characterization of hemoglobins from South Brazilian freshwater teleosts--I. Multiple hemoglobins from the gut/gill breather, Callichthys callichthys.

The five main hemoglobins of the South Brazilian bimodal breathing teleost, Callichthys callichthys were separated, and their oxygenation properties and those of the unfractionated hemolysate were measured at 10, 20 and 30 degrees C. The cathodal Hb component had a higher O2 affinity than the other components and a lower Bohr effect (phi = delta log P 50/delta pH), which is reversed at low and high pH values (6.8 greater than pH greater than 7.8). The other, anodal hemoglobins had normal Bohr effects and similar functional properties. The erythrocytic cofactor ATP had no significant effects on the O2 affinities of the hemolysate and the isolated anodal components at physiological pH conditions, but decreased the affinity of the cathodal Hb over the entire pH range tested (6.5-8.2). All hemoglobins showed high thermal dependence of O2 affinity (delta H values between -62 and -74 kJ mol-1 at pH 8.0), which decreased with falling pH, in accordance with an inverse relation between the Bohr effect and temperature. The possible adaptive significance of the oxygenation patterns of the hemoglobins and their temperature dependences are discussed comparatively with special reference to the closely-related bimodal breather Hoplosternum littorale, and to breathing habit (gill breathing in winter when the fish is a benthic feeder and "gut" air breathing in the warm reproductive season when they nest at the surface).