Membrane-bound proline dehydrogenase from Escherichia coli. Solubilization, purification, and characterization.

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منابع مشابه

Solubilization and partial purification of the membrane-bound hydrogenase of Escherichia coli [proceedings].

Fujita, Y . & Myers, J. (1965) Arch. Biochern. Bioph.ys. 111, 619-625 Gitlitz, P. H. & Krasna, A. I . (1975) Biochemistry 14, 2561-2568 Kakuno, T., Kaplan, N. 0. & Kamen, M. D. (1977)Proc. Not/. Acad. Sci. U.S.A. 71,861-863 Rao, K. K., Rosa, L. & Hall, D. 0. (1976) Biochem. Biophys. Res. Commun. 68, 21-28 Schneider, K. & Schlegel, H. G. (1976) Biochiri?. Biophys. Acfa 452, 66-80 Tel-Or, E., Lui...

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Isolation, Purification and Characterization of Proline Dehydrogenase from a Pseudomonas putida POS-F84 Isolate

The purpose of this study was to isolate and characterize Proline Dehydrogenase (ProDH) enzyme frommicroorganisms isolated from soil in Iran. Isolation and screening of L-proline degradative enzymes from soilsamples was carried out. The isolate was characterized by biochemical markers and 16S rRNA geneanalysis. The target ProDH was purified and the effects of pH and temperatur...

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Purification and properties of D-amino acid dehydrogenase, an inducible membrane-bound iron-sulfur flavoenzyme from Escherichia coli B.

D-Amino acid dehydrogenase, a membrane-associated oxidative enzyme which couples D-alanine oxidation to solute active transport in Escherichia coli B cytoplasmic membrane vesicles, has been solubilized with 0.1% (W/V) Triton X-100 and purified 120-fold from these membranes in the presence of 0.02% Triton X-100 to 265% homogeneity. As isolated, there are 0.8 mg of Triton X-100/mg of enzyme prote...

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Proline dehydrogenase from Escherichia coli K12. Reconstitution of a functional membrane association.

Soluble and membrane associated proline dehydrogenase differ in catalytic properties. The soluble enzyme transfers electrons from L-proline to exogenous electron acceptors. It has a high Km for L-proline (105 mM) and is insensitive to the respiratory chain inhibitors 5-ethyl-5-isopentyl-barbituric acid and cyanide. The membrane-associated enzyme transfers electrons from L-proline to O2 via the ...

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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...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1978

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(17)34569-6