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Am J Physiol Regul Integr Comp Physiol 283: R1052-R1060, 2002. First published August 15, 2002; doi:10.1152/ajpregu.00292.2002
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Vol. 283, Issue 5, R1052-R1060, November 2002

Novel mechanism for high-altitude adaptation in hemoglobin of the Andean frog Telmatobius peruvianus

Roy E. Weber1, Hrvoj Ostojic2, Angela Fago1, Sylvia Dewilde3, Marie-Louise Van Hauwaert3, Luc Moens3, and Carlos Monge4

1 Department of Zoophysiology, University of Aarhus, 131 C. F. Møllers Alle, DK 8000 Aarhus C, Denmark; 2 Clinicum, Laboratorio Automatizado, Iquique, Chile; 3 Biochemistry Department, University of Antwerp, Universiteitsplein 1, B-2610 Antwerpen, Belgium; and 4 Laboratorio de Transporte de Oxígeno, Universidad Cayetano Heredia, Lima 31, Peru

In contrast to birds and mammals, no information appears to be available on the molecular adaptations for O2 transport in high-altitude ectothermic vertebrates. We investigated Hb of the aquatic Andean frog Telmatobius peruvianus from 3,800-m altitude as regards isoform differentiation, sensitivity to allosteric cofactors, and primary structures of the alpha - and beta -chains, and we carried out comparative O2-binding measurements on Hb of lowland Xenopus laevis. The three T. peruvianus isoHbs show similar functional properties. The high O2 affinity of the major component results from an almost complete obliteration of chloride sensitivity, which correlates with two alpha -chain modifications: blockage of the NH2-terminal residues and replacement by nonpolar Ala of polar residues Ser and Thr found at position alpha 131(H14) in human and X. leavis Hbs, respectively. The data indicate adaptive significance of alpha -chain chloride-binding sites in amphibians, in contrast to human Hb where chloride appears mainly to bind in the cavity between the beta -chains. The findings are discussed in relation to other strategies for high-altitude adaptations in amphibians.

amphibians; chloride binding; hypoxia; organic phosphates; oxygen transport


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