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Preferential sulfoxidation of the methionine residues of glycophorin A
Author(s) -
Hardy Robert E.,
Dill Kilian
Publication year - 1982
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(82)80717-5
Subject(s) - chemistry , trifluoroacetic acid , methionine , hydrogen peroxide , glycophorin , reagent , nuclear magnetic resonance spectroscopy , molecule , urea , amino acid , biochemistry , organic chemistry , membrane
Carbon‐13 nuclear magnetic resonance spectroscopy was used to monitor the preferential sulfoxidation of the two methionine residues (8 and 81) of glycophorin A. In urea Met‐8 is readily oxidized. However, Met‐81 can only be oxidized in trifluoroacetic acid containing hydrogen peroxide. Our results also give some insight into the reagent accessibility of different portions of the protein molecule and the general stability of this glycoprotein.