Structural and functional interdependence of the protomers of Escherichia coli K 12 tryptophanase during binding of pyridoxal 5'-phosphate.
Open Access
- 1 May 1976
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 251 (9) , 2814-2819
- https://doi.org/10.1016/s0021-9258(17)33561-5
Abstract
No abstract availableThis publication has 12 references indexed in Scilit:
- Interactions between aspartate aminotransferase protomers observed during holoenzyme reconstitutionBiochemical and Biophysical Research Communications, 1975
- Kinetic and equilibrium studies on the activation of Escherichia coli K12 tryptophanase by pyridoxal 5'-phosphate and monovalent cations.Journal of Biological Chemistry, 1975
- Purification of E. coli enzymes by chromatography on amphiphilic gelsFEBS Letters, 1975
- The apo/holo hybrid of cytosolic aspartate aminotransferase, preparation and studies on subunit interactionsBiochemical and Biophysical Research Communications, 1974
- The Tryptophanase from Escherichia coli K12Published by Elsevier ,1974
- Interaction between Pyridoxamine 5′‐Phosphate and Apo‐Aspartate Aminotransferase from Pig HeartEuropean Journal of Biochemistry, 1972
- Subunit structure of the B component of Escherichia coli tryptophan synthetaseBiochemistry, 1969
- The Subunit Structure of TryptophanasePublished by Elsevier ,1967
- Synthesis and properties of some N-pyridoxyl-l-amino acids and N-(5-phosphopyridoxyl)-l-amino acidsArchives of Biochemistry and Biophysics, 1967
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951