Protein reducing agents dithiothreitol and tris(2-carboxyethyl)phosphine anodic oxidation

[1]  A. Oliveira‐Brett,et al.  Boron doped diamond and glassy carbon electrodes comparative study of the oxidation behaviour of cysteine and methionine. , 2011, Bioelectrochemistry.

[2]  E. Paleček,et al.  Protein structure-sensitive electrocatalysis at dithiothreitol-modified electrodes. , 2010, Journal of the American Chemical Society.

[3]  P. Maeng,et al.  A method for direct application of human plasmin on a dithiothreitol-containing agarose stacking gel system. , 2005, Journal of biochemistry and molecular biology.

[4]  René Kizek,et al.  Cyclic voltammetric study of the redox system of glutathione using the disulfide bond reductant tris(2-carboxyethyl)phosphine. , 2004, Bioelectrochemistry.

[5]  E. Vasini,et al.  A study of the anodic voltammetric properties of triphenylphosphine , 1994 .

[6]  Joan C. Han,et al.  A procedure for quantitative determination of tris(2-carboxyethyl)phosphine, an odorless reducing agent more stable and effective than dithiothreitol. , 1994, Analytical biochemistry.

[7]  Christopher M.A. Brett,et al.  Electrochemistry: Principles, Methods, and Applications , 1993 .

[8]  G. Whitesides,et al.  SELECTIVE REDUCTION OF DISULFIDES BY TRIS(2-CARBOXYETHYL) PHOSPHINE , 1991 .

[9]  W. Cleland,et al.  A specific and sensitive assay for disulfides. , 1968, The Journal of biological chemistry.

[10]  W. Cleland.  DITHIOTHREITOL, A NEW PROTECTIVE REAGENT FOR SH GROUPS. , 1964, Biochemistry.

[11]  T. Naven,et al.  Proteomics in practice : a laboratory manual of proteome analysis , 2002 .