Abstract
AbstractA method for the reduction of methionine sulphoxide to methionine using titanium trichloride is described. This method, coupled with the gas chromatographic determination of methionine after reaction with CNBr, measures methionine sulphoxide by the increase in methionine values after reduction with titanium trichloride. Results obtained for total methionine by gas chromatography after reduction and CNBr reaction, showed close agreement with those obtained by ion‐exchange chromatography after performic acid oxidation. This method was applied to pure proteins which had been subjected to hydrogen peroxide oxidation, and to a wide range of food proteins. An evaluation of other, but less effective, reducing agents is briefly discussed.
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