| Literature DB >> 2950851 |
S Chaudhuri, J M Lambert, L A McColl, J R Coggins.
Abstract
A procedure has been developed for the purification of 3-dehydroquinase from Escherichia coli. Homogeneous enzyme with specific activity 163 units/mg of protein was obtained in 19% overall yield. The subunit Mr estimated from polyacrylamide-gel electrophoresis in the presence of sodium dodecyl sulphate was 29,000. The native Mr, estimated by gel permeation chromatography on Sephacryl S-200 (superfine) and on TSK G3000SW, was in the range 52,000-58,000, indicating that the enzyme is dimeric. The catalytic properties of the enzyme have been determined and shown to be very similar to those of the biosynthetic 3-dehydroquinase component of the arom multifunctional enzyme of Neurospora crassa.Entities:
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Year: 1986 PMID: 2950851 PMCID: PMC1147342 DOI: 10.1042/bj2390699
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857