Results 301 to 310 of about 275,260 (323)
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Preparative affinity precipitation of L-lactate dehydrogenase
Journal of Biotechnology, 1989Abstract The methoxylated p-sulphonate isomer of the triazine dye C.I. Reactive Blue 2, selectively precipitates L-lactate dehydrogenase from crude rabbit muscle extracts. At mildly alkaline pH values and a 7-fold molar excess of the dye analogue to enzyme subunits, 106 mg of homogeneous lactate dehydrogenase essentially free of soluble ligands and ...
James C. Pearson +2 more
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Mechanism of allosteric transition of bacterial L-lactate dehydrogenase
Faraday Discussions, 1992The allosteric behaviour of L-lactate dehydrogenase (L-lactate:NAD+oxidoreductase, EC 1.1.1.27, LDH) from Bifidobacterium longum aM101-2 was studied by means of the subunit hybridization technique as well as X-ray crystallography. Homotropic allosteric response of the LDH activity was found against the concentration of its substrate, pyruvate ...
T, Ohta, K, Yokota, T, Minowa, S, Iwata
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Molecular Basis of Allosteric Activation of Bacterial L-Lactate Dehydrogenase
Journal of Molecular Biology, 1993The three-dimensional structure of allosteric L-lactate dehydrogenase from Bifidobacterium longum, the first example of a T-state structure of L-lactate dehydrogenase, has been determined to 2.0 A. A comparative study of this structure with the previously reported R-state structure from Bacillus stearothermophilus has revealed the allosteric activation
S, Iwata, T, Ohta
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Analytica Chimica Acta, 1996
Carbon-based thick-film electrodes employing nicotinamide adenine dinucleotide (NAD+)-dependent dehydrogenases were constructed by screen printing. Cyclic voltammetric and amperometric investigations of the thick-film electrode showed significantly different electrocatalytic properties toward NADH compared to conventional polished electrodes ...
Hyun C Yoon, Hak-Sung Kim
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Carbon-based thick-film electrodes employing nicotinamide adenine dinucleotide (NAD+)-dependent dehydrogenases were constructed by screen printing. Cyclic voltammetric and amperometric investigations of the thick-film electrode showed significantly different electrocatalytic properties toward NADH compared to conventional polished electrodes ...
Hyun C Yoon, Hak-Sung Kim
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Relationship between L-lactate dehydrogenase and multidrug resistance in Staphylococcus xylosus
Archives of Microbiology, 2021Staphylococcus xylosus is a gram-positive bacterium that has attracted much attention due to its increasing clinical appearance, frequently associated with serious multidrug resistance cases. L-lactate dehydrogenase (LDH) has been related to drug resistance in several bacterial species. However, the mechanism of multidrug resistance in S.
Zhongwei Yuan +10 more
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[57] l-Lactate (cytochrome) dehydrogenase (crystalline, yeast)
1966Publisher Summary This chapter discusses the determination of cytochrome b 2 . This enzyme is the L-lactate: cytochrome c oxidoreductase of bakers' yeast. The activity of the enzyme can be followed by the reduction of cytochrome c , methylene blue, 2,6-dichlorophenolindophenol, or ferricyanide with L-lactate as substrate.
R.H. Symons, L.A. Burgoyne
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An NAD+-independent l-lactate dehydrogenase from Rhizopus oryzae
Biochimica et Biophysica Acta (BBA) - Enzymology, 1971Abstract Two distinct lactate dehydrogenases are present in cultures of a lactic acid-producing strain of Rhizopus oryzae. During rapid vegetative growth, when lactic acid is being produced, the mycelium contains an NAD+-dependent lactate dehydrogenase ( l -lactate:NAD+ oxidoreductase, EC 1.1.1.27) which catalyses the reduction of pyruvate to lactate
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Biosensors and Bioelectronics, 1996
Abstract Covalent immobilization of L-lactate oxidase (LOD) with L-lactate dehydrogenase (LDH) on a film tightly bound to an oxygen electrode, for rapid and sensitive L-lactate measurements, is described. Regeneration of L-lactate by substrate recycling provided an amplification of the sensor response, making it possible to decrease the detection ...
Viviane Casimiri, Claude Burstein
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Abstract Covalent immobilization of L-lactate oxidase (LOD) with L-lactate dehydrogenase (LDH) on a film tightly bound to an oxygen electrode, for rapid and sensitive L-lactate measurements, is described. Regeneration of L-lactate by substrate recycling provided an amplification of the sensor response, making it possible to decrease the detection ...
Viviane Casimiri, Claude Burstein
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Enhanced stability of l -lactate dehydrogenase through immobilization engineering
Process Biochemistry, 2016Abstract l - lactate dehydrogenase (LDH) catalyzes the conversion of pyruvate to l -lactate using NADH as a cofactor. In this work, we have optimized the immobilization of LDH from rabbit muscle in glyoxyl-agarose to have an active and stable preparation which is able to synthesize l -lactic acid.
E. Jackson +3 more
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Archives of Biochemistry and Biophysics, 1989
Lactate dehydrogenase (LDH) (EC 1.1.1.27) from soybean (Glycine max) was purified 2360-fold to homogeneity using ion-exchange, hydroxyapatite, affinity, and hydrophobic chromatographies. The molecular weight of the holoenzyme is 150,000 +/- 5000. Two-dimensional (isoelectrofocusing-sodium dodecyl sulfate) gel electrophoresis reveals two polypeptides ...
K, Tihanyi +3 more
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Lactate dehydrogenase (LDH) (EC 1.1.1.27) from soybean (Glycine max) was purified 2360-fold to homogeneity using ion-exchange, hydroxyapatite, affinity, and hydrophobic chromatographies. The molecular weight of the holoenzyme is 150,000 +/- 5000. Two-dimensional (isoelectrofocusing-sodium dodecyl sulfate) gel electrophoresis reveals two polypeptides ...
K, Tihanyi +3 more
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