Perutz & Brunori (1982) proposed that the COOH-terminal His and Ser F9 of the β-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
Tadpole Xenopus laevis hemoglobin. Correlation between structure and functional properties / Brunori, Maurizio; Condò, Sg; Bellelli, Andrea; Giardina, B; Micheli, G.. - In: JOURNAL OF MOLECULAR BIOLOGY. - ISSN 0022-2836. - STAMPA. - 181:(1985), pp. 327-329. [10.1016/0022-2836(85)90097-X]
Tadpole Xenopus laevis hemoglobin. Correlation between structure and functional properties.
BRUNORI, Maurizio;BELLELLI, Andrea;
1985
Abstract
Perutz & Brunori (1982) proposed that the COOH-terminal His and Ser F9 of the β-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 UrodelaI documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
