Harrington J P
Comp Biochem Physiol B. 1986;84(1):111-6. doi: 10.1016/0305-0491(86)90279-8.
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.
在pH 8.6条件下进行的垂直淀粉凝胶电泳显示，王鲑存在广泛的血红蛋白多样性，有几种不同的阴极和阳极血红蛋白成分。阳极血红蛋白成分在王鲑的整个生命周期中都存在。在成年鱼中发现了额外的阴极成分。阴极血红蛋白成分表现出比阳极血红蛋白成分更高的氧亲和力（在13℃、pH 7.3时P50 = 10.2 mmHg）（在13℃时阳极血红蛋白成分的P50 = 21.8 mmHg）。阳极血红蛋白的氧结合对pH、温度、有机磷酸盐（ATP和GTP）以及离子强度敏感；氧与阴极血红蛋白的结合与pH无关，且不受有机磷酸盐影响。在pH 6.0至8.0范围内，阳极血红蛋白成分对热变性的抵抗力较弱。对王鲑分离出的阳极和阴极血红蛋白组分进行等温尿素变性表明，这些血红蛋白在稳定能方面存在内在差异。这些血红蛋白在pH 7.0及以下以及Cl - 浓度增加时会发生自氧化。
