Chloride NMR studies on the zinc-binding site in E. Coli alkaline phosphatase
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference15 articles.
1. Alkaline Phosphatase of Escherichia coli: A Zinc Metalloenzyme*
2. Conformational States of the Subunit of Escherichia coli Alkaline Phosphatase*
3. Hydrogen-ion equilibria of conformational states of Escherichia colialkaline phosphatase
4. The Biosynthesis of Apo- and Metalloalkaline Phosphatases of Escherichia coli
5. Escherichia coli Co(II) Alkaline Phosphatase
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1. Ion Binding in Biological Systems as Studied by NMR Spectroscopy;Methods of Biochemical Analysis;2006-10-31
2. Chloride binding to alkaline phosphatase. 113Cd and 35Cl NMR.;Journal of Biological Chemistry;1984-09
3. Zinc stoichiometry in Escherichia coli alkaline phosphatase. Studies by 31P NMR and ion-exchange chromatography;Biochimica et Biophysica Acta (BBA) - Enzymology;1978-09
4. Fluorescence properties of terbium-alkaline phosphatase;Archives of Biochemistry and Biophysics;1978-08
5. 113Cd NMR as a probe of the active sites of metalloenzymes;Journal of Magnetic Resonance (1969);1978-02
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