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Biophys J. 1998 December; 75(6): 3085–3091. | PMCID: PMC1299979 |
Augmented water binding and low cellular water content in erythrocytes of camel and camelids. P Bogner, P Csutora, I L Cameron, D N Wheatley, and A Miseta Department of Clinical Chemistry, University Medical School at Pécs, Pécs, Ifjuság u. 13. 7643, Hungary. We investigated a link between hemoglobin primary structure, hemoglobin hydrophobicity-hydrophilicity, and erythrocyte water content in various mammalian species. Some hemoglobin molecules, particularly those of the camel and camelids, contain more charged amino acid residues and are more hydrophilic than the hemoglobins of human and a number of other mammalian species. To test the in vivo significance of these alterations of hemoglobin primary structure, we determined the osmotically unresponsive erythrocyte water fractions in mannit solutions of various osmolarities at 4 degreesC. Among the species investigated, the size of the osmotically unresponsive erythrocyte water fraction relates in a positive linear way to hemoglobin hydrophilicity. The extreme low total erythrocyte water content of camel erythrocytes (1.1-1.3 g water/g dry mass) may be explained by a comparatively high osmotically unresponsive erythrocyte water fraction. It is proposed that alterations of hemoglobin sequences of camel and camelids may be the part of a natural selection process aimed at protecting these animals against osmotic dehydration in arid environments. The Full Text of this article is available as a PDF (125K). These references are in PubMed. This may not be the complete list of references from this article. - Bull HB, Breese K. Surface tension of amino acid solutions: a hydrophobicity scale of the amino acid residues. Arch Biochem Biophys. 1974 Apr 2;161(2):665–670. [PubMed]
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