Antartic fish hemoglobins: an outline of the molecular structure and oxygen binding properties.

The oxygen and carbon monoxide binding to erythrocytes, hemolysate and purified hemoglobin components from the blood of four species of Antarctic fishes (Notothenia coriiceps neglecta, Notothenia rossii, Notothenia gibberifrons and Parachaenichthys charcoti) was investigated. The blood from all the fishes studied displayed the Root effect and the functional properties of hemoglobin were found to be finely regulated by pH and organic phosphates. The results presented indicate an important physiological role for the blood pigment of nototheniids and bathydraconids, in spite of the noting fact that they share the habitat of hemoglobin-less fishes. In particular, it is worth noting that these fishes possess the choroid rete, one of the two organs that require the oxygen-pumping mechanism mediated by a Root-effect hemoglobin.