Pulse radiolysis of the eosin-human serum albumin complex
- 1 January 1970
- journal article
- research article
- Published by Royal Society of Chemistry (RSC) in Transactions of the Faraday Society
- Vol. 66, 1472-1484
- https://doi.org/10.1039/tf9706601472
Abstract
The radiolysis of the eosin-human serum albumin (HSA) complex has been investigated with pulse radiolysis and 60Co irradiation. The rate constant for the reaction of e– aq with eosin decreases from (1.94 ± 0.12)× 1010 1/mol s in aqueous solution to (9 ± 1)× 109 1/mol s when the dye is fully bound to HSA at pH12. The reaction leads to the eosin semiquinone which is less strongly complexed to the protein than the dye. The G value for reductive bleaching of the complexed dye by 60Co in the presence of D-glucose is 0.28, which is consistent with the effective encounter cross-section of the dye moiety. The reaction of hydroxyl radicals with HSA leads to a decrease in the ability to bind eosin, associated with the loss of solubility and not a specific attack on the binding sites.Keywords
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