| Autor: |
M A, Azhigirova, E P, Viazova, M G, Vashkevich, L V, Fetisova, N N, Kontuganov |
| Rok vydání: |
1988 |
| Předmět: |
|
| Zdroj: |
Biulleten' eksperimental'noi biologii i meditsiny. 106(9) |
| ISSN: |
0365-9615 |
| Popis: |
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. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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