| Literature DB >> 3883995 |
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.Entities:
Mesh:
Substances:
Year: 1985 PMID: 3883995 PMCID: PMC1144695 DOI: 10.1042/bj2260217
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857