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RESEARCH PRODUCT

THE FINE STRUCTURE OF O2 Hb BINDING IN ANIMALS: SALMO IRIDEUS

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Publisher Summary This chapter discusses the experimental results on study of the fine structure of O 2 Hb binding in animals. It is evident that the n ( S ) function represents a new tool to look at homotropic interactions, both qualitatively and quantitatively. At the moment, there are four applications: (1) study of molecular mechanism; (2) study of effectors, also pharmacological; (3) improved characterization of O 2 Hb binding, also in pathological cases; and (4) comparative studies in animals. Whole blood of fish is also investigated because usually there are found several hemoglobins. During registration of the O 2 binding curve, pH is not kept constant. Assuming that the Donnan factor does not vary greatly, the change of intracellular pH should not exceed 0.75. In trout blood, there exist two sorts of O 2 binding sites in equal parts that bind independently. But each population by itself binds O 2 in a positive cooperative manner. The n -values exceeding 4 make evident a self-association of the tetramer Hb molecules within the erythrocytes.