Functional properties of the glycosylated minor hemoglobins A1a-1,A1a-2 and A1b. EPR evidence for increased stability of the low affinity quaternary structure and decreased susceptibility to organic phosphate.
Electron paramagnetic resonance (EPR) spectra of the glycosylated minor hemoglobins A1a-1, A1a-2, A1b and A1c and the major hemoglobin A0 in the nitrosyl form have been obtained in the absence and presence of inositol hexaphosphate. In the absence of inositol hexaphosphate, nitrosyl hemoglobins A1a-1, A1a-2 and A1b exhibited a triplet hyperfine structure centered at g = 2.009 which has been shown to be diagnostic of the low affinity (T) quaternary structure. Addition of inositol hexaphosphate to nitrosyl hemoglobins A0, A1c, A1b and A1a-2 developed a triplet hyperfine structure of the EPR spectra but the magnitude of the hyperfine was decreased in the order of hemoglobins A0, A1c, A1b and A1a-2. However, inositol hexaphosphate had essentially no effect on the EPR spectrum of nitrosyl hemoglobin A1a-1. The present results account qualitatively for the oxygen binding properties of these glycosylated minor hemoglobins in the framework of a two-state allosteric model.
D000494:Allosteric Regulation; D002263:Carboxyhemoglobin; D004355:Drug Stability; D004578:Electron Spin Resonance Spectroscopy; D006442:Glycated Hemoglobin; D006027:Glycosides; D006441:Hemoglobin A / Q000031:analogs & derivatives*; D006801:Humans; D046911:Macromolecular Substances; D010108:Oxyhemoglobins; D010833:Phytic Acid / Q000097:blood*; D011485:Protein Binding; D011487:Protein Conformation
D002263:Carboxyhemoglobin; D006442:Glycated Hemoglobin; D006027:Glycosides; D006441:Hemoglobin A; D046911:Macromolecular Substances; D010108:Oxyhemoglobins; D010833:Phytic Acid