Perutz & Brunori (1982) proposed that the COOH-terminal His and Ser F9 of the beta-chains of fish and amphibian hemoglobins are responsible for their Root effect and part of their alkaline Bohr effect. Analysis of the kinetics of carbon monoxide binding by hemoglobin from the tadpole of Xenopus laevis supports that model and suggests an explanation for the absence of an alkaline Bohr effect in many aquatic Anura and Urodela.

Brunori, M., Condo', S.g., Bellelli, A., Giardina, B., Micheli, G. (1985). Tadpole Xenopus laevis hemoglobin. Correlation between structure and functional properties. JOURNAL OF MOLECULAR BIOLOGY, 181(2), 327-329.

Tadpole Xenopus laevis hemoglobin. Correlation between structure and functional properties

CONDO', SAVERIO GIOVANNI;
1985-01-20

Abstract

Perutz & Brunori (1982) proposed that the COOH-terminal His and Ser F9 of the beta-chains of fish and amphibian hemoglobins are responsible for their Root effect and part of their alkaline Bohr effect. Analysis of the kinetics of carbon monoxide binding by hemoglobin from the tadpole of Xenopus laevis supports that model and suggests an explanation for the absence of an alkaline Bohr effect in many aquatic Anura and Urodela.
Pubblicato
Rilevanza internazionale
Articolo
Sì, ma tipo non specificato
Settore BIO/10
English
Xenopus laevis; Animals; Hemoglobins; Larva; Hydrogen-Ion Concentration; Carbon Monoxide; Amino Acid Sequence
Brunori, M., Condo', S.g., Bellelli, A., Giardina, B., Micheli, G. (1985). Tadpole Xenopus laevis hemoglobin. Correlation between structure and functional properties. JOURNAL OF MOLECULAR BIOLOGY, 181(2), 327-329.
Brunori, M; Condo', Sg; Bellelli, A; Giardina, B; Micheli, G
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/54859
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