The Chemical Structure of Tryptophanase from Escherichia coli

作者：Hiroyuki Kagamiyama, Yoshimasa Morino, Esmond E. Snell · 发表于：Journal of Biological Chemistry · 年份：1970 · DOI：10.1016/s0021-9258(18)63063-7 · 被引用次数：48 · 研究领域：Protein Hydrolysis and Bioactive Peptides、Enzyme Production and Characterization、Meat and Animal Product Quality

Following reduction with NaBH4, carboxymethylation, and chymotryptic digestion, a decapeptide containing the Ne-pyridoxyllysine residue was isolated from the tryptophanase of Escherichia coli by the consecutive use of Dowex 1 column chromatography, paper chromatography, and high voltage paper electrophoresis. The primary structure of this peptide was determined to be [see PDF for sequence] Its structure differs from those found for the corresponding peptides from other enzymes so far studied.