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|Isohemoglobin differentiation in the bimodal-breathing Amazon catfish Hoplosternum littorale
|Weber, Roy Edwin
Val, Adalberto Luis
van Hauwaert, Marie Louise
Moens, Luc J.
|2,3 Diphosphoglyceric Acid
Amino Acid Sequence
Amino Acid Sequence
Molecular Sequence Data
Sequence Homology, Amino Acid
|Journal of Biological Chemistry
|Volume 275, Número 23, Pags. 17297-17305
|The bimodal gill(water)/gut(air)-breathing Amazonian catfish Hoplosternum littorale that frequents hypoxic habitats uses 'mammalian' 2,3- diphosphoglycerate (DPG) in addition to 'piscine' ATP and GTP as erythrocytic O2 affinity modulators. Its electrophoretically distinct anodic and cathodic hemoglobins (Hb(An) and Hb(Ca) were isolated for functional and molecular characterization. In contrast to Hb(An), phosphate-free Hb(Ca) exhibits a pronounced reverse Bohr effect (increased O2 affinity with decreasing pH) that is obliterated by ATP, and opposite pH dependences of K(T) (O2 association constant of low affinity, tense state) and the overall heat of oxygenation. Dose-response curves indicate small chloride effects and pronounced and differentiated phosphate effects, DPG < ATP < GTP < IHP. Hb(Ca)-O2 equilibria analyzed in terms of the Monod-Wyman-Changeux model show that small T state bond energy differences underlie the differentiated phosphate effects. Synthetic peptides, corresponding to N-terminal fragment of the cytoplasmic domain of trout band 3 protein, undergo oxygenation-linked binding to Hb(Ca), suggesting a metabolic regulatory role for this hemoglobin. The amino acid sequences for the α and β chains of Hb(Ca) obtained by Edman degradation and cDNA sequencing show unusual substitutions at the phosphate-binding site that are discussed in terms of its reverse Bohr effect and anion sensitivities.
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