Summary
A chromatographic method is described for the isolation of the methionine-bound sulfur in casein for stable-isotope-ratio analysis. Casein is cleaved by acid hydrolysis and the high-molecular-weight secondary products formed are removed by adsorption on octadecyl-silica. Methionine is separated from the bulk of the polar amino acids by cation-exchange chromatography and subsequently oxidized to methionine sulfone by performic and peracetic acid. In a further step the methionine is isolated from the accompanying nonpolar amino acids by cation-exchange chromatography with a mobile phase of very low eluent strength.
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Lamprecht, G., Pichlmayer, F. & Schmid, E.R. Cation-exchange chromatographic isolation of the methionine-bound sulfur in casein hydrolysates for stable-isotope-ratio analysis. Chromatographia 47, 271–277 (1998). https://doi.org/10.1007/BF02466531
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DOI: https://doi.org/10.1007/BF02466531