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Am J Physiol Regul Integr Comp Physiol (August 15, 2002). doi:10.1152/ajpregu.00292.2002
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Articles in PresS, published online ahead of print August 15, 2002
Am J Physiol Regu Physiol, 10.1152/ajpregu.00292.2002
Submitted on May 23, 2002
Accepted on July 9, 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, Aarhus, Denmark
2 Laboratorio Automatizado, Clinicum, Iquique, Chile
3 Biochemistry Department, University of Antwerp, Antwerp, Belgium
4 Laboratorio de Transporte de Oxigeno, Universidad Cayetano Heredia, Lima, Peru

* To whom correspondence should be addressed. E-mail: roy.weber{at}biology.au.dk.

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 hemoglobin (Hb)of the aquatic Andean frog Telmatobius peruvianus from 3800 m altitude as regards isoform differentiation, sensitivity to allosteric cofactors and primary structures of the {alpha} and ß chains, and 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 N-terminal residues, and replacement by nonpolar Ala of polar residues Ser and Thr, at position {alpha}131(H14) in human and X. leavis hemoglobins, respectively. The data indicate adaptive significance of {alpha}-chain chloride-binding sites in amphibians, in contrast to human hemoglobin where chloride appears mainly to bind in the cavity between the ß chains. The findings are discussed in relation to other strategies for high-altitude adaptations in amphibians.




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