Equilibria and kinetics of oxygen and carbon monoxide binding to the haemoglobin of the teleost Synbranchus marmoratus

1. 1. The haemoglobins of the air-breathing fish Synbranchus marmoratus have multiple components and demonstrate polymorphism. 2. 2. The equilibrium of oxygen with whole cell and isolated haemoglobin has been compared. There is a considerable alkaline Bohr effect and this is more marked in stripped haemoglobin to which 1 mM ATP has been added. 3. 3. The kinetics of oxygen dissociation from oxyhaemoglobin and of carbon monoxide combination to deoxyhaemoglobin have been studied, and show surprisingly uniform kinetic time courses for a system composed of multiple components. 4. 4. These findings are discussed within the framework of the requirements of the animal in its mixed aerial-aquatic environment.