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J Appl Physiol 38: 806-810, 1975;
8750-7587/75 $5.00
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Journal of Applied Physiology, Vol 38, Issue 5 806-810, Copyright © 1975 by American Physiological Society

ARTICLES

Oxygen transport of hemoglobin in high-altitude animals (Camelidae)

C. Reynafarje, J. Faura, D. Villavicencio, A. Curaca, B. Reynafarje, L. Oyola, L. Contreras, E. Vallenas and A. Faura

To clarify the mechanisms by which high-altitude Camelidae can adapt to hypoxia, the study of some blood characteristics were carried out in apacas and llamas. The results show that there is a peculiar dissociation curve of hemoglobin in alpacas which permits great affinity of hemoglobin for oxygen at lung level and the release of oxygen at the tissue level with a facility similar to that in man. Fetal hemoglobin was found high in adult alpacas (55 percent). Electrophoretic studies of hemoglobin showed that this pigment has two components, both of which have a very low mobility. Lactic dehydrogenase was found six times higher than in humans. RBC glucose-6-phosphate dehydrogenase was two times higher than in man living at the same altitude. Myoglobin was found to be higher than in man living at altitude. Alpacas have erythrocytes in which the amount of 2,3-DPG is approximately the same as in man. RBC are more resistent to hypotonic solutions than humans. The amount of lactic dehydrogenase, myoglobin, and glucose-6-phosphate dehydrogenase dimishes when alpacas are bought down to sea level.


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