title: [Biochemical properties of intramolecularly cross-linked hemoglobin].
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.
authors.forename: M A
authors.initials: MA
authors.lastname: Azhigirova
authors.forename: E P
authors.initials: EP
authors.lastname: Viazova
authors.forename: M G
authors.initials: MG
authors.lastname: Vashkevich
authors.forename: L V
authors.initials: LV
authors.lastname: Fetisova
authors.forename: N N
authors.initials: NN
authors.lastname: Kontuganov
mesh_terms: 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
chemical_list: D001802:Blood Substitutes; D003432:Cross-Linking Reagents; D006454:Hemoglobins
vernacular_title: Biokhimicheskie svoĭstva vnutrimolekuliarno sshitogo gemoglobina.