An investigation of the allosteric functioning of the haemoglobin of the cane toad, Bufo marinus.
1. Cane toad haemoglobin shows co-operative equilibrium CO binding at pH 7.0 with n = 2.6. 2. Flash photolysis studies show that at high pH the R form of the protein is stabilised whilst low pH and the presence of IHP favours the T form. 3. The combination of stopped-flow and flash photolysis measurements allows estimation of the association and dissociation rates of CO binding for the two forms of the protein. 4. The protein functioning can be described by a modified two state model and mathematical modelling allows the estimation of the allosteric equilibrium constant for this haemoglobin.
D000818:Animals; D002024:Bufo marinus; D002248:Carbon Monoxide / Q000378:metabolism; D006454:Hemoglobins / Q000378:metabolism / Q000502:physiology*; D007700:Kinetics; D008433:Mathematics
D006454:Hemoglobins; D002248:Carbon Monoxide