Abstract
The chemical modification of hemoglobin was conducted with the help of bifunctional crosslinking agent--glutaraldehyde. By SDS-polyacrylamide gel electrophoresis and gel-filtration it was shown that the final product contained 70% of modified protein which consisted of non-dissociating hemoglobin dimers and tetramers. It was also shown that the chemical modification didn't produce significant changes in the oxygen-transporting properties of the starting hemoglobin, but had influence on the character of the interaction with the allosteric regulator of reversible oxygenation (pyridoxal-5'-phosphate). The half-disappearance period in animals of the intramolecularly crosslinked hemoglobin was two times longer in comparison with the native protein.
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