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1 Hemoglobin Structure And Function

F. Jensen, A. Fago, R. Weber
Published 1998 · Biology

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This chapter describes the hemoglobin (Hb) structure and function in fishes. Hb of most vertebrates is a tetrameric globular protein consisting of two α and two β polypeptide chains, each having an oxygen-binding heme. The oxygen affinity of Hb varies with globin structure, giving rise to species differences that relate to differences in primary structure. The hydrogen ion equilibria of Hb are fundamental to both the structure and the physiological function of the protein. The exchange of H + between protein and solvent is important for blood CO 2 transport and it makes Hb an effective nonbicarbonate buffer that limits fluctuations in blood pH upon acid or base additions. The acidic carboxyl groups of glutamic acid and aspartic acid residues are negatively charged at physiological pH and are titrated only when pH falls below 6. Basic groups, such as the guanidyl group of arginine and the amino group of lysine side chains, are positively charged at physiological pH and release H + only when the pH exceeds above 9. It is found that the fixed acid Haldane effect is generally large in teleosts, but differs among species.
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