Refolding and Reactivation of Escherichia coli Tryptophan Synthase beta2 Subunit after Inactivation and Dissociation in Guanidine Hydrochloride at Acidic pH
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1978.tb12764.x/fullpdf
Reference16 articles.
1. Cooperative and noncooperative binding of pyridoxal 5'-phosphate to tryptophan synthase from Escherichia coli
2. Association of β-chain monomers of Escherichia coli tryptophan synthetase
3. Subunit structure of the B component of Escherichia coli tryptophan synthetase
4. Kinetic studies of tryptophan synthetase. Interaction of substrates with the B subunit
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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