Abstract
Hemoglobin molecules after digestion with carboxypeptidase A or B show large differences in their ligand affinity, heme-heme interaction, Bohr effect and response to organic phosphates. Removal of β146 histidine and β145 tyrosine produces a molecule of high oxygen affinity, low Bohr effect and no heme-heme interaction. Removal of α141 arginine produces similar, but less drastic, changes. In both digestion products normal functional behavior may be partially restored by addition of inositol hexaphosphate. Doubly digested hemoglobins (carboxypeptidase A followed by B or vice versa) have properties similar to the initial digestion products but are no longer responsive to organic phosphates. The equilibrium and kinetic properties of these proteins are presented and are consistent with the idea that various conformations of the unliganded molecules may be in equilibrium.
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