The formation of dehydroalanine residues in alkali-treated insulin and oxidized glutathione. A nuclear-magnetic-resonance study
- 1 May 1983
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 211 (2) , 499-502
- https://doi.org/10.1042/bj2110499
Abstract
1H- and 13C-NMR measurements enable direct observation of the rate of formation of dehydroalanine residues resulting from lysis of the S-S bonds of [pig] insulin and oxidized glutathione in base at pD 13. The data provide clear evidence for the .beta.-elimination mechanism for this reaction. The dehydroalanine-containing products from the lysis of insulin undergo secondary reactions.This publication has 8 references indexed in Scilit:
- Metabolic Interrelations of Sulfur in Proteins, Thiosulfate, and CystinePublished by Elsevier ,2021
- Nuclear-Magnetic-Resonance-Spectroscopic Studies of the Amino Groups of InsulinEuropean Journal of Biochemistry, 1977
- The preparation and subsequent identification of a dehydroalanyl peptide from alkali-treated oxidised glutathioneBiochimica et Biophysica Acta (BBA) - Protein Structure, 1972
- Alkaline hydrolysis of the disulfide bonds of ovomucoid and of low molecular weight aliphatic and aromatic disulfidesBiochemistry, 1971
- Kinetic studies on the alkaline decomposition of cystine derivatives and peptidesJournal of the American Chemical Society, 1967
- Nδ-(2d-amino-2-carboxyethyl)-ornithine, a New Amino-acid from Alkali-treated ProteinsNature, 1967
- NEPSILON-(DL-2-AMINO-2-CARBOXYETHYL)-L-LYSINE NEW AMINO ACID FORMED ON ALKALINE TREATMENT OF PROTEINS1964
- The Sulfur Chemistry of ProteinsAdvances in Protein Chemistry, 1959