Purification of serine acetyltransferase, a component of a multienzyme complex, by immunoadsorption and selective dissociation of the complex
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference12 articles.
1. Purification and Characterization of Cysteine Synthetase, a Bifunctional Protein Complex, from Salmonella typhimurium
2. The Purification and Characterization of O-Acetylserine Sulfhydrylase-A from Salmonella typhimurium
3. A reaction mechanism from steady state kinetic studies for O-acetylserine sulfhydrylase from Salmonella typhimurium LT-2.
4. Initial kinetic characterization of the multienzyme complex, cysteine synthetase
5. The Enzymic Synthesis of l-Cysteine in Escherichia coli and Salmonella typhimurium
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2. Combination of SAXS and Protein Painting Discloses the Three-Dimensional Organization of the Bacterial Cysteine Synthase Complex, a Potential Target for Enhancers of Antibiotic Action;International Journal of Molecular Sciences;2019-10-21
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5. Cysteine biosynthesis inLactobacillus casei: identification and characterization of a serine acetyltransferase;FEMS Microbiology Letters;2016-01-19
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