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- W2025677254 abstract "The automatic method described by Piez and Morris (2) has been used with slight modifications to effect a complete resolution of S-carboxyethylcysteine. This allows for the direct quantitation of the compound and facilitates the use of its protein precursor, S-cyanoethylcysteine, in compositional and structural studies. It has been demonstrated that 100% of the disulfide and/or thiol groups of proteins can be determined by alkylation of the reduced proteins with acrylonitrile, followed by acid hydrolysis. It has also been shown that acrylonitrile is a nonspecific alkylating agent for at least three milk proteins under specified conditions and that up to 45% of the lysine residues may be alkylated. Further, for S-cyanoethyl-β-lactoglobulin AB and for S-cyanoethyl-κ-casein, at least two new ninhydrin-positive peaks occur in two different chromatographic systems after acid hydrolysis of the proteins. These peaks are presumed to be related to the decrease in lysine." @default.
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- W2025677254 date "1965-09-01" @default.
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- W2025677254 title "The determination of S-carboxyethylcysteine and the cyanoethylation of milk proteins" @default.
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- W2025677254 doi "https://doi.org/10.1016/0003-2697(65)90215-0" @default.
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