PROTEIN METABOLISM IN REGENERATING WOUND TISSUE FUNCTION OF THE SULFUR AMINO ACIDS.
Abstract
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)
Document Details
- Document Type
- Technical Report
- Publication Date
- May 31, 1967
- Accession Number
- AD0654449
Entities
People
- Martin B. Williamson
Organizations
- Loyola University Chicago