Abstract
The course and mechanism of reaction of ninhydrin with amines has both bioanalytical and bioorganic significance since the reaction is widely used for analysis of amino groups and serves as a model for several biochemical reactions that occur in metabolism of phosphonic acid derivatives, deamination, transamination, and transpeptidation. In many cases, e.g., with lysine, cysteine, proteins, the yield of the ninhydrin product, Ruhemann's purple, does not correspond exactly to the expected 1 equiv. per amino group. Possible reasons for this apparent nonideal stoichiometry include slow formation, side reactions, hydrolytic, oxidative, and photolytic instability, and interfering color. The origin and contributions of each of these factors are examined.
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