The purification of shikimate dehydrogenase from Escherichia coli
- 15 February 1985
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 226 (1) , 217-223
- https://doi.org/10.1042/bj2260217
Abstract
A procedure was developed for the purification of shikimate dehydrogenase from E. coli. Homogeneous enzyme with specific activity 1100 U/mg of protein was obtained in 21% overall yield. The subunit MW estimated by polyacrylamide-gel electrophoresis in the presence of sodium dodecyl sulfate was 32,000. The native MW 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.This publication has 28 references indexed in Scilit:
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