Carbon-2 proton exchange at histidine-41 in bovine erythrocyte superoxide dismutase
Keyword(s):
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.
1978 ◽
Vol 43
(6)
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pp. 439-449
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1973 ◽
Vol 248
(12)
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pp. 4229-4234
1974 ◽
Vol 249
(22)
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pp. 7339-7347
Keyword(s):
1993 ◽
Vol 60
(4)
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pp. 1274-1282
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