Purification of 5-enolpyruvylshikimate 3-phosphate Synthase from Escherichia Coli
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A procedure for the purification of 5-enolpyruvylshikimate 3-phosphate synthase from Escherichia coli is described. Homogeneous enzyme of specific activity 17.7 units/mg was obtained in 22% yield. The key purification step involves substrate elution of the enzyme from a cellulose phosphate column. The subunit Mr was estimated to be 49 000 by polyacrylamide-gel electrophoresis in the presence of sodium dodecyl sulphate. The native Mr was estimated to be 55 000 by gel filtration, indicating that the enzyme is monomeric.
Ding D, Liu Y, Xu Y, Zheng P, Li H, Zhang D Sci Rep. 2016; 6:32208.
PMID: 27558633 PMC: 4997321. DOI: 10.1038/srep32208.
Mousdale D, Coggins J Planta. 2013; 160(1):78-83.
PMID: 24258375 DOI: 10.1007/BF00392469.
Powell H, Kerby N, Rowell P, Mousdale D, Coggins J Planta. 2013; 188(4):484-90.
PMID: 24178379 DOI: 10.1007/BF00197039.
Ream J, Steinrucken H, Porter C, Sikorski J Plant Physiol. 1988; 87(1):232-8.
PMID: 16666109 PMC: 1054731. DOI: 10.1104/pp.87.1.232.
Rubin J, Gaines C, Jensen R Plant Physiol. 1984; 75(3):839-45.
PMID: 16663714 PMC: 1067003. DOI: 10.1104/pp.75.3.839.