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Tadpole Xenopus laevis hemoglobin. Correlation between structure and functional properties |
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| Authors: | M Brunori S G Condò A Bellelli B Giardina G Micheli |
| Institution: | 1. Institute of Chemistry, Faculty of Medicine and CNR Center of Molecular Biology University of Rome “La Sapienza” Italy;2. Department of Experimental Medicine and Biochemical Sciences, University of Rome “Tor Vergata”, 00185 Rome, Italy |
| 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. |
| Keywords: | Author to whom all correspondence should be addressed at: Istituto di Chimica Facoltà di Medicina e Chirurgia Université “La Sapienza” 00185 Rome Italy |
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