O-Sulphate esters of l-serine, l-threonine and l-hydroxyproline

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Abstract
Methods have been described for the preparation of the O-sulphate esters of L-serine, L-threonine and L-hydroxyproline. The esters exhibit a similar stability towards acid, but L-serine and L-threonine O-sul-phates are much less stable to alkali than the corresponding L-hydroxyproline derivative. Enzymic sulphation of the 3 amino acids by a rat-liver system known to be capable of sulphating other hydroxylated compounds could not be achieved. Rat liver contains an enzyme system, the activity of which results in the liberation of inorganic sulphate from L-serine O-sulphate. Maximum enzyme activity is obtained in the region of pH 7.0.