Source:http://linkedlifedata.com/resource/pubmed/id/21356843
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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
2011-3-1
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pubmed:abstractText |
INTRODUCTIONThis protocol describes a method for performing reduction and S-alkylation of Coomassie-blue-stained proteins within an intact gel. Reduction is performed with dithiothreitol, and alkylation with 4-vinylpyridine. (Treatment of free cysteines with 4-vinylpyridine yields the S-?-(4-pyridylethyl) cysteinyl derivative.) S-?-(4-pyridylethyl) cysteine-containing peptides can be readily identified during RP-HPLC by their characteristic absorbance at 254 nm and during electrospray ionization tandem mass spectrometry by the appearance of a characteristic pyridylethyl fragment ion of 10(6) Da. The position of cysteine residues in a polypeptide sequence can be determined either by mass spectrometry or as phenylthiohydantoin S-?-(4-pyridylethyl) cysteine during Edman degradation.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:status |
PubMed-not-MEDLINE
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pubmed:author | |
pubmed:volume |
2008
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
pdb.prot4604
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pubmed:year |
2008
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pubmed:articleTitle |
In-gel s-pyridylethylation of gel-resolved proteins: whole gel method.
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pubmed:publicationType |
Journal Article
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