Identification of peptides containing tryptophan, tyrosine, and phenylalanine using photodiode-array spectrophotometry |
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| Authors: | C Y Yang H J Pownall A M Gotto |
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| Affiliation: | 1. Baylor College of Medicine, Houston, Texas 77030 USA;2. The Methodist Hospital, Houston, Texas 77030 USA;1. Hubei Collaborative Innovation Center for Advanced Organic Chemical Materials, Ministry of Education Key Laboratory for the Green Preparation and Application of Functional Materials, Hubei Key Laboratory of Polymer Materials, Faculty of Materials Science and Engineering, Hubei University, Wuhan, China;2. Key Laboratory of Functional Small Organic Molecule, Ministry of Education; Key Laboratory of Green Chemistry, Jiangxi Province and College of Chemistry and Chemical Engineering, Jiangxi Normal University, Nanchang, China;1. Institute of Food Science and Biotechnology, Department of Soft Matter Science and Dairy Technology, University of Hohenheim, Garbenstr. 21, 70593 Stuttgart, Germany;2. Institute of Food Chemistry, Leibniz Universität Hannover, Callinstr. 5, 30167 Hannover, Germany;3. Institute of Food Science and Biotechnology, Department of Food Physics and Meat Science, University of Hohenheim, Garbenstr. 25, 70593 Stuttgart, Germany;1. University of Colorado, Boulder, CO 80309, United States;2. NASA Ames Research Center, Moffett Field, CA 95032, United States |
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| Abstract: | The characteristic absorption spectra of aromatic amino acids between 240 and 310 nm were used to identify tryptophan, tyrosine, and phenylalanine-containing peptides. In acidic solution, the absorption spectra of these amino acids exhibit minima or maxima at 255, 270, and 286 nm. Based on these characteristics, the content of the aromatic amino acid in peptide can be estimated. For this study, 2 nmol of tryptic peptides from human apolipoprotein A-1 was separated by high-performance liquid chromatography using a reverse-phase column. The peptide fragments were monitored by a photodiode-array spectrophotometer. This new approach offers a rapid, simple, sensitive, and direct identification of peptides containing aromatic amino acids. Those containing Trp, which may be of interest for DNA sequencing and important in sequence analysis of proteins, can be selectively purified using this technique. |
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