Abstract
Summary
The reaction of 35S-cystine with sulfhydryl groups of both native and denatured proteins is inhibited in the presence of low concentrations of glutamic acid. Identical inhibitory activity is displayed by N-substituted derivatives of this amino acid, but not by derivatives in which either carboxylic acid group is blocked. Aspartic acid does not interfere with this reaction. The effect of glutamic acid is greatest at pH 7.4 and decreases markedly in more acidic or more basic media. It is suggested that glutamic acid may regulate metabolic processes by affecting the activity of sulfhydryl-activated enzymes.
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