Oxygen transport and acid-base balance in the blood of the sheatfish, Silurus glanis.

Oxygen binding and buffer properties of the blood of the sheatfish, Silurus glanis, were investigated in vitro at 20 and 10 degrees C. The O2 binding curves were hyperbolic with P50 = 10.1 mm Hg (20 degrees C, pH = 7.5) and 4.6 (10 degrees C, pH = 7.5). There was a very large Bohr effect with an average delta log P 50/delta pH of - 1.14. At 20 degrees C this value tended to be higher than at 10 degrees C. As a consequence the apparent heat of oxygenation depended on pH. The mean value of delta H was -10.4 kcal/mol. The Haldane effect was pronounced too (delta pH/delta S = -0.14) as was the Root effect. Isoelectric focussing revealed 3 major hemoglobin fractions with isoionic points in a more alkaline region than in carp hemoglobin. The non-bicarbonate buffer value was -10 mmol . 1-1. pH -1. The intraerythrocytic pH depended on the extracellular pH and the O2 saturation: pH = (0.87 - 0.14 S) (pHe -6.68 + 6.48). Delta pH/delta t for a constant CO2 content was -0.0166.