PMID:3883995

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Citation

Chaudhuri, S and Coggins, JR (1985) The purification of shikimate dehydrogenase from Escherichia coli. Biochem. J. 226:217-23

Abstract

A procedure was developed for the purification of shikimate dehydrogenase from Escherichia coli. Homogeneous enzyme with specific activity 1100 units/mg of protein was obtained in 21% overall yield. The subunit Mr estimated by polyacrylamide-gel electrophoresis in the presence of sodium dodecyl sulphate was 32 000. The native Mr, estimated by gel-permeation chromatography on a TSK G2000SW column, was also 32 000. E. coli shikimate dehydrogenase is therefore a monomeric NADP-linked dehydrogenase.

Links

PubMed PMC1144695

Keywords

Alcohol Oxidoreductases/isolation & purification; Chromatography, Gel; Chromatography, Ion Exchange; Electrophoresis, Polyacrylamide Gel; Escherichia coli/enzymology

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