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Molecular adaptation of the blood of Antarctic teleosts to environmental conditions

Published online by Cambridge University Press:  14 May 2004

Guido Di Prisco
Affiliation:
Institute of Protein Biochemistry and Enzymology, CNR, Via Toiano 6, 80072 Arco Felice, Naples, Italy
Rossana D'Avino
Affiliation:
Institute of Protein Biochemistry and Enzymology, CNR, Via Toiano 6, 80072 Arco Felice, Naples, Italy

Abstract

Following the break-up of Gondwana, the drift of Antarctica to its present position and the establishment of the Antarctic Convergence, fish evolution was characterized by adaptation to progressive cooling of the environment. The decrease of erythrocyte number and haemoglobin concentration in the blood of Antarctic teleosts raises several questions concerning the physiology of respiration and the enzymatic role of erythrocytes. Our study of the molecular basis of cold adaptation includes the relationship between molecular structure and biological function of haemoglobins. Species of the suborder Notothenioidei, largely confined within the Convergence, have only one major haemoglobin, which displays the Root effect in oxygen binding; on the other hand, Zoarcidae (a family found at all latitudes) have four or five haemoglobins, only one of which displays the Root effect. In addition, our data indicate that the physiological relevance of erythrocyte-like cells, present in very small number in the blood of haemoglobinless Channichthyidae, may be linked to higher content of enzymes, such as glucose-6-phosphate dehydrogenase, in comparison with erythrocytes of red-blooded fishes.

Type
Papers—Life Sciences and Oceanography
Copyright
© Antarctic Science Ltd 1989

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