[Keto acids as regulators of hemoglobin reversible oxygenation]

Several ketocarbonic acids covalently attached to the protein moiety of hemoglobin were tested as reversible oxygenation regulators. Two monocarbonic acids (glycoxylic and piruvic) and bicarbonic--alpha-ketoglutaric-acid were used for remoglobin modification. Functional properties and isoelectrical characteristics of modified hemoglobin were recorded. The binding of these acids to hemoglobin was shown to affect the net charge of hemoglobin molecule and the nature of its interaction with allosteric effectors (O2; CI-; H+). Under the influence of glyoxylic acid, the gas-transporting characteristics of hemoglobin underwent most distinct changes approaching those of the human whole blood.