Oxygen effect in the radiolysis of proteins. III. Haemoglobin.
Radiolysis of haemoglobin was carried out in phosphate buffer under air, N2 or N2O and with and without ethanol. Radiation products were separated by SDS-PAGE. The loss of subunits and simultaneous aggregation and fragmentation of haemoglobin was measured, if OH-radicals were unscavenged. There was no sensitizing effect of oxygen on the degradation process. Radiation-induced fragmentation was not a random process, but produced specific fragments. The estimated molecular weights of these fragments gave further support to the assumption that the aminoacyl-proline peptide group is the preferential breaking site if OH radicals react with proteins in the presence of oxygen. In contrast with lactate dehydrogenase and bovine serum albumin such fragmentation was observed not only after aerobic radiolysis but also under anaerobic conditions. This difference must be caused by the Feporphyrin system which reacts with H2O2 under release of oxygen. If haemoglobin was irradiated under air the yield of aggregates was much lower than under N2O or N2.
Puchała
M
M
University of Lodź, Poland.
Schuessler
H
H
D004591:Electrophoresis, Polyacrylamide Gel; D000431:Ethanol / Q000494:pharmacology; D006454:Hemoglobins / Q000528:radiation effects*; D006801:Humans; D008970:Molecular Weight; D009584:Nitrogen / Q000494:pharmacology; D009609:Nitrous Oxide / Q000494:pharmacology; D010100:Oxygen / Q000494:pharmacology*; D010108:Oxyhemoglobins / Q000528:radiation effects
D006454:Hemoglobins; D010108:Oxyhemoglobins; D000431:Ethanol; D009609:Nitrous Oxide; D009584:Nitrogen; D010100:Oxygen