Peculiarities of Structure, Polymorphism, and Resistance to Oxidation of Fish Hemoglobins

The paper presents data on peculiarities of structural organization of fish hemoglobin molecules. The existence of symmetric and asymmetric complexes and their importance for formation in some types of complex heterogeneous hemoglobin systems is considered. The comparative characteristics of the primary structure of - and -chains of the respiratory pigments in higher and lower vertebrates are presented. The causes of low resistance of fish hemoglobins to oxidation are discussed. Protective action of Cl^– under conditions of nitrite intoxication, as well as role of several intraerythrocytic molecular systems in maintaining the pigment ferroform (superoxide dismutase, catalase, peroxidase, and NADH-diaphorase) are considered.