A new reagent for the routine identification of cysteine residues during protein sequencing is described. This method employs 3-bromopropylamine to alkylate cysteines in proteins after reduction with dithiothreitol. Upon sequencing of the protein on an Applied Biosystems 477 A protein sequencer, the
Alkylation of cysteine with acrylamide for protein sequence analysis
โ Scribed by Daniel C. Brune
- Publisher
- Elsevier Science
- Year
- 1992
- Tongue
- English
- Weight
- 649 KB
- Volume
- 207
- Category
- Article
- ISSN
- 0003-2697
No coin nor oath required. For personal study only.
๐ SIMILAR VOLUMES
HepG2 lysates. As expected, the highest signal was found for the liver cell line (24). The proposed assay is highly sensitive and allows screening of high numbers of samples in an easy and rapid way. All these characteristics together make the Determination of Cysteine Residues in Protein test very
Methods are given for determination of the phenylthiohydantoin derivative of pyridylethylcysteine (PTH-PECys) by gas chromatography, both with and without prior trimethylsilylation. Using the high-cysteine polypeptide purothionin, obtained from wheat, as a model system, cysteine residues at positio
It is recognised that gel-separated proteins can experience a frequent modification provoked by the interaction of unpolymerized acrylamide monomers with the thiol group of cysteine to form a beta-cysteinyl-S-propionamide adduct. Other groups which have been implicated in this reaction include the h