[Biochemical properties of intramolecularly cross-linked hemoglobin].
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.
Azhigirova
M A
MA
Viazova
E P
EP
Vashkevich
M G
MG
Fetisova
L V
LV
Kontuganov
N N
NN
D000818:Animals; D001797:Blood Protein Electrophoresis; D001802:Blood Substitutes; D002850:Chromatography, Gel; D003432:Cross-Linking Reagents; D006207:Half-Life; D006454:Hemoglobins / Q000032:analysis*; D006801:Humans; D007525:Isoelectric Focusing; D008970:Molecular Weight; D051381:Rats
D001802:Blood Substitutes; D003432:Cross-Linking Reagents; D006454:Hemoglobins
Biokhimicheskie svoĭstva vnutrimolekuliarno sshitogo gemoglobina.