Abstract
The C-2 proton of one histidine residue in bovine erythrocyte superoxide dismutase is shown to be particularly labile. This residue is identified by tritiation, protein digestion and subsequent peptide 'mapping' as histidine-41. A half-life for the exchange of histidine C-2 1H for 2H in 2H2O as solvent, at pD 8.1 and 40 degrees C, is estimated as approx. 9.2h, by 1H nuclear-magnetic-resonance spectroscopy.
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Selected References
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