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Direct Electrochemistry of Native and Denatured Anticancer Antibody Rituximab at a Glassy Carbon Electrode
Author(s) -
Oliveira Severino Carlos B.,
Santarino Inês B.,
OliveiraBrett Ana Maria
Publication year - 2013
Publication title -
electroanalysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.574
H-Index - 128
eISSN - 1521-4109
pISSN - 1040-0397
DOI - 10.1002/elan.201200552
Subject(s) - chemistry , tryptophan , tyrosine , sodium dodecyl sulfate , histidine , dithiothreitol , glassy carbon , phosphinate , transmembrane protein , biochemistry , electrochemistry , biophysics , electrode , amino acid , cyclic voltammetry , organic chemistry , biology , receptor , fire retardant , enzyme
Rituximab (RTX) is a human/murine chimeric monoclonal antibody (mAb) that specifically targets the transmembrane protein CD20 of B‐cells. The oxidation mechanism of native and denatured RTX was investigated on glassy carbon electrode. The denaturing agent sodium dodecyl sulfate and the redutancts tris(2‐carboxyethyl)phosphine and dithiothreitol were used. Significant differences were observed for native and denatured RTX oxidation due to morphological changes and unfolding of the RTX native structure. Native RTX presented only one oxidation peak of tyrosine and tryptophan residues, whereas in denatured RTX were detected three peaks corresponding to the oxidation of tyrosine, tryptophan and histidine residues.