The hemoglobin system of the primitive fish, Amia calva: isolation and functional characterization of the individual hemoglobin components.
Biochim Biophys Acta
; 434(1): 18-31, 1976 May 20.
Article
em En
| MEDLINE
| ID: mdl-938661
ABSTRACT
Blood from the primitive holostean fish, the bowfin, Amia calva, contains 2 mo of ATP per mol of hemoglobin. The hemolysates contain at least five tetrameric hemoglobin components which differ in their oxygen affinities and their response to cofactors such as ATP. The binding of oxygen by each chromatographically isolated component, including a cathodal component, is influenced by pH and organic phosphates; there is no significant differentiation of function or structure as seen in trout and certain other fish hemolysates. Kinetic analyses of ligand binding indicate that the Bohr and Root effects of Amia calva hemoglobins are best explained by changes in both the "on" and "off" constants. At low pH, the increase in the "off" constant is smaller than for most other Root hemoglobins. The hemoglobin system of Amina calva is functionally undifferentiated and may be representative of the ancestral condition in teleosts.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Hemoglobinas
/
Peixes
Limite:
Animals
Idioma:
En
Ano de publicação:
1976
Tipo de documento:
Article