PROTEIN METABOLISM IN REGENERATING WOUND TISSUE FUNCTION OF THE SULFUR AMINO ACIDS.
Annual rept. 1 Jun 66-31 May 67,
LOYOLA UNIV CHICAGO ILL STRITCH SCHOOL OF MEDICINE
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The reaction of 35S-cystine with sulfhydryl groups and of reduced 35S-glutathione with disulfide groups in 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 glutamic acid, but not by derivatives in which either carboxyl group is blocked. Aspartic acid does not interfere with the exchange reaction. The effect of glutamic acid is greatest at pH 7.3-7.5, but decreases markedly in more acidic or more basic solution. It is proposed that glutamic acid may act as an important regulator of metabolic processes by affecting the enzymes which are activated or inhibited by the sulfhydryl-disulfide exchange reaction. Author
- Medicine and Medical Research