An investigation of the co-operative binding of carbon monoxide to the haemoglobin of the carpet shark Cephaloscyllium.
1. Carpet Shark haemoglobin shows co-operative equilibrium CO binding at pH 7.0 (n = 1.8). 2. Flash photolysis shows that the T form of the protein is stabilised at low pH and in the presence of Inositol Hexaphosphate (I.H.P.). 3. At high pH the R form of the protein is stabilised and exhibits kinetic heterogeneity, assigned to different chain reactivities. 4. Stopped flow and flash photolysis under various conditions allows estimates to be made of the association and dissociation rates of CO binding for the two forms of the protein. 5. The functionality of the protein, with regard to CO binding, can be described by a modified two state model.
D000494:Allosteric Regulation; D000818:Animals; D002248:Carbon Monoxide / Q000097:blood*; D006454:Hemoglobins / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D007700:Kinetics; D008024:Ligands; D011485:Protein Binding; D012754:Sharks / Q000097:blood*
D006454:Hemoglobins; D008024:Ligands; D002248:Carbon Monoxide