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Subunit structure of the tryptophan synthetase of Escherichia coli
Authors:M E Goldberg  T E Creighton  R L Baldwin  C Yanofsky
Affiliation:1. Department of Pediatrics, Jichi Medical University, Tochigi, Japan;2. Department of Pediatrics, Toyonaka Municipal Hospital, Osaka, Japan;3. Department of Pediatrics, Tokyo Metropolitan Fuchu Ryoiku Center, Tokyo, Japan;4. Department of Metabolism, Chiba Children''s Hospital, Chiba, Japan.;5. Department of Pediatrics & Clinical Genomics, Faculty of Medicine, Saitama Medical University, Saitama, Japan;6. Center for Intractable Diseases, Saitama Medical University Hospital, Saitama, Japan;7. Diagnostics and Therapeutics of Intractable Diseases, Intractable Disease Research Center, Graduate School of Medicine, Juntendo University, Tokyo, Japan;8. Department of Life Science, Faculty of Science and Engineering, Kindai University, Osaka, Japan.;9. Department of Pediatrics, Teikyo University School of Medicine, Tokyo, Japan.;10. Department of Human Genetics, Yokohama City University Graduate School of Medicine, Yokohama, Japan;11. Department of Human Genetics, Research Institute, National Center for Global Health and Medicine, Tokyo, Japan.;12. Laboratory for Comprehensive Genomic Analysis, RIKEN Center for Integrative Medical Sciences, Kanagawa, Japan;13. Department of Pediatrics, Gunma University Graduate School of medicine, Maebashi, Japan
Abstract:In order to determine the subunit composition of the tryptophan synthetase of Escherichia coli, the molecular weights of the β2 subunit and of the (α + β) complex have been measured by ultracentrifugation. The weight ratio in which the α and β2 subunits combine has been determined by sedimentation velocity and by amino acid analysis. The results agree very well with an α2β2 structure.The possibility of forming an αβ2 structure has been examined and conditions have been found in which this structure is stable.
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