Results 211 to 220 of about 183,054 (259)
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Journal of Biotechnology, 2009
D-form lactate is often found in fermented foods and excessive dietary intake of D-lactate may cause metabolic stress in both infants and patients. Leuconostoc citreum is a major lactic acid bacterium that produces D-lactate in fermented foods. The aim of this study was to change the pyruvate carbon flux in L.
Qing, Jin +6 more
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D-form lactate is often found in fermented foods and excessive dietary intake of D-lactate may cause metabolic stress in both infants and patients. Leuconostoc citreum is a major lactic acid bacterium that produces D-lactate in fermented foods. The aim of this study was to change the pyruvate carbon flux in L.
Qing, Jin +6 more
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Electron microscopic observations of l-lactate dehydrogenase crystals
Journal of Ultrastructure Research, 1969Thin sections and shadowed replicas of dogfish muscle lactate dehydrogenase crystals were examined in the electron microscope. The observed periodicities are in good agreement with the X-ray data. The density variations in the stained thin sections can be explained using the X-ray determined molecular structure.
L W, Labaw, M G, Rossmann
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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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Low resolution study of crystalline l-lactate dehydrogenase
Journal of Molecular Biology, 1969The electron density distribution of dogfish muscle lactate dehydrogenase, based on 2000 independent terms extending to 5 A resolution, shows the shape of the tetrameric molecule and of the individual subunits. Each of the five heavy-atom derivatives used in the calculation substitutes at one or more of three sites A, B and C. The heavy-atom compounds (
M J, Adams +7 more
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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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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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L(+)‐lactate dehydrogenases from Hymenolepis diminuta (Cestoda)
Journal of Experimental Zoology, 1973AbstractProperties of L( + )‐lactate dehydrogenases from infective eggs, cysticercoids, immature proglottids (anteriors), and pre‐patent (seven day) infections of H. diminuta were studied. Fractionation of isozymes by disc gel and cellulose acetate electrophoresis was unsatisfactory, but some fractionation was obtained by electrofocusing.
M, Walkey, D, Fairbairn
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Negative entropy production in L-lactate dehydrogenase kinetics
Archive of Biochemistry, 2023Fröhlich theory of coherent excitations in biological systems is analyzed. L-lactate dehydrogenase kinetics is studied using the activation process model for non-equilibrium cases. The model explains the process of energy accumulation necessary for carrying out catalytic reactions in a living cell by means of interaction of quantum subsystems with ...
Stepanov AV, Stepanov MA
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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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Cloning and characterization of l-lactate dehydrogenase gene of Staphylococcus aureus
Anaerobe, 2013Staphylococcus aureus a natural inhabitant of nasopharyngeal tract survives in the host as biofilms. In the present study S. aureus ATCC12600 grown under anaerobic conditions showed biofilm units of 0.086 as compared to 0.07 when this pathogen grown in aerobic conditions with elevated lactate formation and the same was also observed with increased ...
Sthanikam, Yeswanth +5 more
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