4-Vinylpyridine is used as a derivatizing reagent for free thiols such as GSH. It is used in the Glutathione colorimetric assay to remove reduced GSH, so that the oxidized Glutathione (GSSG) concentration can be measured. 4-Vinylpyridine is a better derivatizing reagent for GSH when compared to N-ethyl-maleimide (NEM) as N-ethyl-maleimide is a potent inhibitor of glutathione reductase. The treatment of samples with 4-vinylpyridine removes all the free thiols present in the sample leaving only GSSG which can be quantified in the same way as total glutathione using Ellman’s Reagent.
4-Vinylpyridine alkylates cysteine and cystine residues (after reduction) in proteins to give derivatives that are stable to acid hydrolysis and so it is used in analysis of proteins2. Its alkylating property also enables it to be used for preparation of proteins from PAGE for peptide mapping by MALDI-MS and MALDI-TOF.
- 4-Vinylpyridine supplied in low volumes. This feature enables better handling of this flammable product. In addition for derivatization of GSH for oxidized glutathione assay, low concentrations of 4-Vinylpyridine are needed.
- It can be used as derivatizing agent for free thiols or alkylating agent depending upon requirements.
- Molecular formula: C7H7N
- Molecular weight: 105.1
- CAS #: 100-43-6
- Density: 0.975 g/ml
- Removes GSH in samples so that oxidized glutathione concentration can be measured.
- It can be used in protein structure analysis as it alkylates cysteine and cystine residues (after reduction) in proteins to give derivatives that are stable to acid hydrolysis.
- It can be used for preparation of proteins from PAGE for maximal recovery for peptide mapping by MALDI-MS and MALDI-TOF.
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- Griffith O. W. (1980). Determination of glutathione and glutathione disulfide using glutathione reductase and 2-vinylpyridine. Analytical biochemistry 106, 207-212.
- Friedman M. (2001). Application of the S-pyridylethylation reaction to the elucidation of the structures and functions of proteins. J Protein Chem. 20,431-453.
- Ming, D. et al. (1995). Quantification of cysteinyl sulfhydryl residues in peptides and proteins by ESI-MS or MALDI-MS. Biotechnoques 18,808-810.
- Sechi, S. and Chait, B. T. (1998). Modification of cysteine residues by alkylation. A tool in peptide mapping and protein identification. Anal. Chem. 70(4), 5150-5158.