Isolated alpha and beta chains from Xenopus laevis hemoglobin have been purified. The isolation procedure yields native alpha chains whose functional behavior has been characterized and compared with that of human alpha chains. Isolated beta chains in the presence of oxygen are characterized by low stability, and hence their functional characterization was limited to the CO binding kinetics. When stoichiometric amounts of the isolated alpha and beta chains are mixed, a tetramer characterized by heme-heme interactions and oxygen affinity comparable to that of the native molecule is readily reconstituted. Moreover, both chains, under appropriate conditions, form stable hybrid tetramers with the partner subunits from human hemoglobin; results on the functional properties of these hybrid hemoglobins are presented and discussed in relation to the stereochemical model of the Root effect.

Condo', S.g., Giardina, B., Bellelli, A., Brunori, M. (1987). Xenopus laevis hemoglobin and its hybrids with hemoglobin A+. BIOCHEMISTRY, 26(21), 6718-6722.

Xenopus laevis hemoglobin and its hybrids with hemoglobin A+

CONDO', SAVERIO GIOVANNI;
1987-10-20

Abstract

Isolated alpha and beta chains from Xenopus laevis hemoglobin have been purified. The isolation procedure yields native alpha chains whose functional behavior has been characterized and compared with that of human alpha chains. Isolated beta chains in the presence of oxygen are characterized by low stability, and hence their functional characterization was limited to the CO binding kinetics. When stoichiometric amounts of the isolated alpha and beta chains are mixed, a tetramer characterized by heme-heme interactions and oxygen affinity comparable to that of the native molecule is readily reconstituted. Moreover, both chains, under appropriate conditions, form stable hybrid tetramers with the partner subunits from human hemoglobin; results on the functional properties of these hybrid hemoglobins are presented and discussed in relation to the stereochemical model of the Root effect.
Pubblicato
Rilevanza internazionale
Articolo
Sì, ma tipo non specificato
Settore BIO/10
English
Animals; Electrophoresis, Starch Gel; Oxyhemoglobins; Humans; Hydrogen-Ion Concentration; Hemoglobin A; Electrophoresis, Cellulose Acetate; Isoelectric Focusing; Protein Multimerization; Macromolecular Substances; Xenopus laevis; Hemoglobins; Kinetics
Condo', S.g., Giardina, B., Bellelli, A., Brunori, M. (1987). Xenopus laevis hemoglobin and its hybrids with hemoglobin A+. BIOCHEMISTRY, 26(21), 6718-6722.
Condo', Sg; Giardina, B; Bellelli, A; Brunori, M
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/54854
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