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. 1983 Jul 1;213(1):187–191. doi: 10.1042/bj2130187

Purification of 5-enolpyruvylshikimate 3-phosphate synthase from Escherichia coli.

A Lewendon, J R Coggins
PMCID: PMC1152107  PMID: 6351837

Abstract

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.

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Selected References

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