THE BLOOD PROTEINS OF THE ANTARCTIC ICEFISH CHANNICHTHYS-RHINOCERATUS - BIOLOGICAL SIGNIFICANCE AND PURIFICATION OF THE 2 MAIN COMPONENTS

peer reviewed The lack of hemoglobin and of carbonic anhydrase in the blood of icefish suggest that substantial adaptations of the acid-base balance should 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...

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Bibliographic Details
Published in:Comparative Biochemistry and Physiology Part B: Comparative Biochemistry
Main Authors: Feller, Georges, Poncin, Alain, Aittaleb, M., Schyns, R., Gerday, Charles
Format: Article in Journal/Newspaper
Language:English
Published: Elsevier Science 1994
Subjects:
ICEFISH
CHANNICHTHYS RHINOCERATUS
NOTOTHENIA ROSSII
ANTARCTIC
HYPOXIA RESISTANCE
PARA-ALBUMIN
FISH IMMUNOGLOBULINS
ACID-BASE
BALANCE
NON-BICARBONATE BUFFER
FISH CHAENOCEPHALUS-ACERATUS
HEMOGLOBIN-FREE FISH
TROUT
SALMO-GAIRDNERII
SERUM
HEART
MYOGLOBIN
ALBUMIN
HYPOXIA
Life sciences
Biochemistry
biophysics & molecular biology
Sciences du vivant
Biochimie
biophysique & biologie moléculaire
Antarctic
The Antarctic
Antarc*
Icefish
Notothenia rossii
Online Access:https://orbi.uliege.be/handle/2268/15257
https://doi.org/10.1016/0305-0491(94)90145-7
Description
Summary:peer reviewed The lack of hemoglobin and of carbonic anhydrase in the blood of icefish suggest that substantial adaptations of the acid-base balance should 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 common red-blooded Antarctic species. It is proposed that the high level of imidazole ring in icefish plasma improves the non-bicarbonate buffering capacity and that the reactive sulfhydryls are involved om a redox buffer as in some other hypoxia tolerant species. After plasma fractionation on Ultrogel AcA 34, the two main icefish serum proteins have been purified by DEAE cellulose chromatography (IFI) and by HPLC on anion exchange column (IF2). IFI has been identified as a cysteine-rich para-albumin and IF2 as an histidine-rich immunoglobulin-like protein.

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