Multiplicity of phosphorylation sites onEscherichia coli isocitrate dehydrogenase |
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Authors: | Jean-Claude Cortay Dr. Henry C. Reeves Alain J. Cozzone |
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Affiliation: | (1) Laboratory of Molecular Biology, University of Lyon, Villeurbanne, France;(2) Department of Botany and Microbiology, Arizona State University, 85287 Tempe, Arizona, USA |
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Abstract: | Several lines of evidence indicate that the in vivo phosphorylation of isocitrate dehydrogenase (EC 1.1.1.42) inEscherichia coli occurs at multiple sites: first, the phosphorylated enzyme can be resolved by two-dimensional electrophoresis into three distinct spots differing in charge; second, the analysis of its phosphoamino acid content shows that it is modified at both serine and threonine residues; third, its extensive hydrolysis by proteolytic enzymes yields several different phosphopeptides. |
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