Tadpole Xenopus laevis hemoglobin. Correlation between structure and functional properties.
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.
D000595:Amino Acid Sequence; D000818:Animals; D002248:Carbon Monoxide / Q000378:metabolism; D006454:Hemoglobins / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007814:Larva; D014982:Xenopus laevis / Q000254:growth & development
D006454:Hemoglobins; D002248:Carbon Monoxide