Purification and Properties of 5,10-Methylenetetrahydrofolate Dehydrogenase from Escherichia coli
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چکیده
منابع مشابه
Purification and properties of lactaldehyde dehydrogenase from Escherichia coli.
An aldehyde dehydrogenase capable of acting on Llactaldehyde was detected in a strain of Escherichia coli K-12 selected to grow on 1,2-propanediol as the sole source of carbon and energy. This enzyme activity was purified over 200-fold by ammonium sulfate fractionation followed by diethylaminoethyl cellulose chromatography, Sephadex G-100 gel flltration, and DEAE-Sephadex chromatography. The pu...
متن کاملPurification and properties of NADH-dependent 5, 10-methylenetetrahydrofolate reductase (MetF) from Escherichia coli.
A K-12 strain of Escherichia coli that overproduces methylenetetrahydrofolate reductase (MetF) has been constructed, and the enzyme has been purified to apparent homogeneity. A plasmid specifying MetF with six histidine residues added to the C terminus has been used to purify histidine-tagged MetF to homogeneity in a single step by affinity chromatography on nickel-agarose, yielding a preparati...
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The membrane-bound formate dehydrogenase of Escherichia coli grown anaerobically in the presence of nitrate was solubilized with deoxycholate and purified to near homogeneity. The purification procedure included ammonium sulfate fractionation and chromatography on Bio-Gel A-1.5m and DEAE Bio-Gel A in the presence of the nonionic detergent, Triton X-100. This detergent caused a significant decre...
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The L-glycerol-3-phosphate: NAD(P) oxidoreductase (EC 1.1.1.8). referred to as glycerol phosphate dehydrogenase, was purified from extracts of Escherichia coli by a combination of chromatographic procedures. The over-all purification was approximately lOOO-fold and the yield was about 10%. The elution profile from the final DEAE-Sephadex column and zone electrophoresis indicated that the enzyme...
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L-Threonine dehydrogenase, which catalyzes the conversion of L-threonine to aminoacetone + CO2 presumably via the intermediate formation of alpha-amino-beta-ketobutyrate, has been purified to apparent homogeneity from extracts of a mutant of Escherichia coli K-12 which has constitutively derepressed levels of the enzyme. Three fractionation steps were used including controlled heat denaturation...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1965
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)97081-x