The dissociation of human deoxyhemoglobin and mixed state hemoglobin into monomer.
The experimental hybridizations between fully deoxygenated human and canine hemoglobins and between half-ligated human hemoglobin and canine cyanomethemoglobin show that new two hybrids in addition to the parent hemoglobins were clearly formed in the mixtures at the high concentration of KI. Thus, human deoxyhemoglobin under the present conditions is in an equilibrium with three species, tetramer in equilibrium dimer in equilibrium monomer. This means that the deoxyhemoglobin is in R-T equilibrium, and shifts considerably toward the R state under the present conditions. On the other hand, the half-ligated hemoglobin in 1.5 M KI becomes much more dissociable than the deoxy T state and appears to be completely transformed into the R state. Nevertheless, the co-operativity, n, is still high (n = 2.0).
D000818:Animals; D001665:Binding Sites; D003486:Cyanides / Q000097:blood; D004228:Dithionitrobenzoic Acid; D004285:Dogs; D006454:Hemoglobins; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007454:Iodides / Q000097:blood; D007700:Kinetics; D046911:Macromolecular Substances; D008970:Molecular Weight; D011485:Protein Binding
D003486:Cyanides; D006454:Hemoglobins; D007454:Iodides; D046911:Macromolecular Substances; D004228:Dithionitrobenzoic Acid