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Cation-exchange chromatographic isolation of the methionine-bound sulfur in casein hydrolysates for stable-isotope-ratio analysis (1998)

Lamprecht, G. ; Pichlmayer, F. ; Schmid, E. R.

Springer

Chromatographia 47 (1998), S. 271-277

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Details

ISSN: 1612-1112

Schlagwort(e): Column Liquid chromatography ; Cation-exchange chromatography ; Sulfur stable-isotope-ratio analysis ; Casein hydrolysate ; Methionine

Quelle: Springer Online Journal Archives 1860-2000

Thema: Chemie und Pharmazie

Notizen: 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.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1007/BF02466531

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