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- W1512647055 abstract "Publisher Summary This chapter describes the cysteine (Cys) modification with acrylonitrile for amino acid analysis and protein sequencing. Unmodified Cys is not detected during analysis of amino acids derivatized with the fluorogenic reagent o -phthaldialdehyde (OPA). Thus, Cys is converted to derivatives that give fluorescent products upon reaction with OPA. The methods include performic acid oxidation to cysteic acid, disulfide exchange, and alkylation with 4-vinylpyridine. The chapter presents the experiments where insulin, containing three disulfide bonds, is reduced by tributylphosphine (BU 3 P) and alkylated by acrylonitrile in the presence of ammonium bicarbonate buffer, pH 8.5. All of these reagents, including the buffer, are volatile and thus can be removed from the protein during the normal vacuum drying prior to hydrolysis. The time course of the reaction is monitored by laser desorption time-of-flight mass spectrometry to obtain conditions resulting in complete Cys alkylation and a minimum of side reactions. In addition, acrylonitrile is used in place of acrylamide as a Cys alkylating agent prior to protein sequencing and gives a well-resolved and easily identified derivative." @default.
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- W1512647055 date "1996-01-01" @default.
- W1512647055 modified "2023-09-27" @default.
- W1512647055 title "Cysteine modification with acrylonitrile for amino acid analysis and protein sequencing" @default.
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- W1512647055 doi "https://doi.org/10.1016/s1080-8914(96)80027-5" @default.
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