Structural and functional studies of the king salmon, Oncorhynchus tshawytscha, hemoglobins.

Vertical starch-gel electrophoresis at pH 8.6 revealed extensive hemoglobin multiplicity with several distinct cathodal and anodal hemoglobin components. Anodal hemoglobin components are present throughout the life cycle of the king salmon. Additional cathodal components are found in the adult fish. Cathodal hemoglobin components exhibited a higher oxygen affinity (P50 = 10.2 mm at 13 degrees C, pH 7.3) than the anodal hemoglobin components (P50 = 21.8 mmHg at 13 degrees C). Oxygen binding of the anodal hemoglobins are sensitive to pH, temperature, organic phosphates (ATP and GTP), as well as, ionic strength; binding of oxygen to the cathodal hemoglobins is independent of pH and not affected by organic phosphates. Anodal hemoglobin components are less resistant to thermal denaturation over the pH 6.0 to 8.0 range. Isothermal urea denaturation of separated anodal and cathodal hemoglobin fractions of the king salmon indicate inherent differences in the stabilization energies of these hemoglobins. Autoxidation of these hemoglobins occurs around pH 7.0 and below, as well as, in the presence of increasing Cl- concentrations.