Cobalt(III) affinity-labeled aspartokinase. Formation of substrate and inhibitor adducts
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00662a010
Reference27 articles.
1. Cobalt(III), a probe of metal binding sites of Escherichia coli alkaline phosphatase.
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3. A Study of the Interaction of Manganese Ions with ATP by 31P Fourier-Transform Nuclear-Magnetic Resonance
4. Affinity Labeling of the Adenosine 5′-Monophosphate Binding Site of Rabbit Muscle Glycogen Phosphorylase b with an Adenosine 5′-Monophosphate-Cobalt(III) Complex
5. Threonine-sensitive aspartokinase from Escherichia coli. Magnetic resonance and binding studies
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2. Labeling of integrin alpha v beta 3 with 58Co(III). Evidence of metal ion coordination sphere involvement in ligand binding;Journal of Biological Chemistry;1991-06
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4. Fluorescence studies of threonine-promoted conformational transitions in aspartokinase I using the substrate analogue 2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-triphosphate.;Journal of Biological Chemistry;1983-11
5. Characterization of proteolysis fragments of aspartokinase I: homoserine dehydrogenase I. Fluorescence and circular dichroism studies.;Journal of Biological Chemistry;1983-11
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