Studies on the functional properties of fish hemoglobins. II. The oxygen equilibrium of the isolated hemoglobin components from trout blood.

@article{Binotti1971StudiesOT,
  title={Studies on the functional properties of fish hemoglobins. II. The oxygen equilibrium of the isolated hemoglobin components from trout blood.},
  author={I. Binotti and S. Giovenco and B. Giardina and E. Antonini and M. Brunori and J. Wyman},
  journal={Archives of biochemistry and biophysics},
  year={1971},
  volume={142 1},
  pages={
          274-80
        }
}
Homogeneous components of trout hemoglobin (Salmo irideus) have been isolated by column chromatography. The oxygen equilibrium of the two main components has been investigated. The oxygen affinity and the shape of the ligand equilibrium curve is independent of pH for component I. On the other hand, component IV is characterized by a very large Bohr effect, to which a considerable change in the shape of the oxygen equilibrium curve with pH is associated. The different oxygen-binding… Expand
Studies on the properties of fish hemoglobins. Kinetics of reaction with oxygen and carbon monoxide of the isolated hemoglobin components from trout (Salmo irideus).
TLDR
The Root effect characteristic of Hb trout IV appears to originate, from a kinetic point of view, in a pH-dependent change of both the “on” and “off” constants, although at least for O2 the effect of pH on the ‘off’ kinetic constants is much more marked. Expand
Studies on the properties of fish hemoglobins. Molecular properties and interaction with third components of the isolated hemoglobins from trout (Salmo irideus).
TLDR
The effect of several third components on the O2 equilibrium of both Hb trout I and IV has been investigated and a clear cut effect of Hp binding is observed on the kinetics of O2 and especially CO combination as studied by flash photolysis. Expand
Observations on CO trout hemoglobins by 13C NMR
TLDR
The ’ 3C n.r.m. spectra of the 13C0 bound to both I-lb trout I and Hb trout IV are determined to gain a better insight in the molecular mechanism operative in the hemoglobin components from trout. Expand
Redox properties of components I and IV of trout hemoglobins: kinetic and potentiometric studies.
TLDR
Differently from human hemoglobin, the oxidation kinetics of the two hemoglobins from trout by potassium ferricyanide show markedly biphasic progress curves with pH-independent second-order rate constants, which suggests a different energy barrier for the interaction with fericyanide in the two types of subunit of both Hb components from trout. Expand
Trout hemoglobin: Oxygen binding at sub‐zero temperatures
TLDR
The data now available do not allow to exclude an effect of protons in enhancing such an intrinsic functional difference between the OL and p subunits within the hemoglobin molecule, and intramolecular analysis is recommended. Expand
Functional properties of partially oxidized trout hemoglobins.
TLDR
The results of the O2 equilibria and of CO binding kinetics may be interpreted in accordance with the two state concerted model suggesting that in the oxidation intermediates there is an increase in the fraction of the high affinity (R) conformation. Expand
Effect of anions on the oxygen binding properties of the hemoglobin components from trout (Salmo irideus).
TLDR
Investigation of the effect of several anions on the oxygen equilibrium of hemoglobin components from trout finds various phosphates shift the region where the Root effect is operative toward higher pH values, thereby acting as allosteric effectors. Expand
Hemoglobin in fishes: Structural and functional properties of trout hemoglobins
Abstract Homogeneous components of trout hemoglobin (Salmo irideus), have been investigated from the structural and functional point of view. Only one (Hb trout IV) of the 2 major components found inExpand
The hemoglobin system of the primitive fish, Amia calva: isolation and functional characterization of the individual hemoglobin components.
TLDR
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. Expand
Molecular adaptation to physiological requirements: the hemoglobin system of trout.
  • M. Brunori
  • Biology, Medicine
  • Current topics in cellular regulation
  • 1975
TLDR
On the basis of the behavior of the isolated hemoglobin components from trout blood and of their distribution among the erythrocytes, it has been possible to provide a “rationale” for the existence of several hemoglobins. Expand
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