Cooperative Binding of alpha Subunits to the Apo-beta2 Subunit of Tryptophan Synthase from Escherichia coli
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1979.tb12968.x/fullpdf
Reference32 articles.
1. Subunit structure of the tryptophan synthetase of Escherichia coli
2. Association of the α and β2 Subunits of the Tryptophan Synthetase of Escherichia coli
3. Purification and Properties of the B Component of Escherichia coli Tryptophan Synthetase
4. Tryptophan synthase of Escherichia coli. Removal of pyridoxal 5'-phosphate and separation of the alpha and beta2 subunits.
5. The Tryptophan Synthase from Escherichia coli. An Improved Purification Procedure for the alpha-Subunit and Binding Studies with Substrate Analogues
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1. Ligand binding and unfolding of tryptophan synthase revealed by ion mobility-tandem mass spectrometry employing collision and surface induced dissociation;International Journal for Ion Mobility Spectrometry;2013-03-23
2. Negative Cooperativity in Tryptophan Synthase α Subunit Dissociation Is Caused by the Bound Coenzyme: Pyridoxal 5′-Phosphate;Analytical Biochemistry;1998-11
3. Dissociation equilibria of the tryptophan synthase α2β2 complex in saline buffer and guanidine isothiocyanate, as studied by sedimentation equilibrium;Biophysical Chemistry;1997-11
4. Subunit Assembly in the Tryptophan Synthase α2β2 Complex;Journal of Biological Chemistry;1995-04
5. Influence of .alpha.-Subunits on the High-Pressure Stability of Apo and Holo .beta.2-Subunits in the Bienzyme Complex Tryptophan Synthase from Escherichia coli;Biochemistry;1995-02-14
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