G. Feller et al., THE BLOOD PROTEINS OF THE ANTARCTIC ICEFISH CHANNICHTHYS-RHINOCERATUS- BIOLOGICAL SIGNIFICANCE AND PURIFICATION OF THE 2 MAIN COMPONENTS, Comparative biochemistry and physiology. B. Comparative biochemistry, 109(1), 1994, pp. 89-97
The lack of hemoglobin and of carbonic anhydrase in the blood of icefi
sh suggest that substantial adaptations of the acid-base balance shoul
d occur in order to ensure blood pH homeostasis. The level of peptidic
histidyl and of reactive -SH groups per unit of body mass in icefish
plasma are 12-13 times higher that those of Notothenia rossii, a commo
n red-blooded Antarctic species. It is proposed that the high level of
imidazole ring in icefish plasma improves the non-bicarbonate bufferi
ng capacity and that the reactive sulfhydryls are involved om a redox
buffer as in some other hypoxia tolerant species. After plasma fractio
nation on Ultrogel AcA 34, the two main icefish serum proteins have be
en purified by DEAE cellulose chromatography (IFI) and by HPLC on anio
n exchange column (IF2). IFI has been identified as a cysteine-rich pa
ra-albumin and IF2 as an histidine-rich immunoglobulin-like protein.