Results 311 to 320 of about 414,201 (353)
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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 (
Michael G. Rossmann +7 more
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Journal of Biochemistry (Tokyo), 1982
Heat-stable L-lactate dehydrogenase [EC 1.1.1.27] was purified from an extremely thermophilic bacterium belonging to the genus Thermus, and it showed an allosteric nature dependent on fructose 1,6-bisphosphate as an effector.
H. Taguchi +3 more
semanticscholar +1 more source
Heat-stable L-lactate dehydrogenase [EC 1.1.1.27] was purified from an extremely thermophilic bacterium belonging to the genus Thermus, and it showed an allosteric nature dependent on fructose 1,6-bisphosphate as an effector.
H. Taguchi +3 more
semanticscholar +1 more source
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.
Hyun-Ju Eom +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.
Hyun-Ju Eom +6 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
Takahisa Ohta, So Iwata
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The complete primary structure of the allosteric L-lactate dehydrogenase from Lactobacillus casei.
European Journal of Biochemistry, 1983The polypeptide chain of the allosteric L-lactate dehydrogenase (EC 1.1.1.27) of Lactobacillus casei consists of 325 amino acid residues. Despite the strikingly different enzymatic characteristics of the allosteric L-lactate dehydrogenase of L. casei and
R. Hensel, U. Mayr, C. Yang
semanticscholar +1 more source
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.
Donald Fairbairn, Michael Walkey
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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 ...
Uppu Venkateswara Prasad +5 more
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European Journal of Biochemistry, 1980
The allosteric L-lactate dehydrogenases of Lactobacillus curvatus and Lactobacillus casei exist in the tetrameric from (molecular weight about 145 000) at pH 5.0--5.5 even in the absence of the effectors Mn2+ and Fru(1,6)P2 (fructose 1,6-bisphosphate ...
U. Mayr, R. Hensel, O. Kandler
semanticscholar +1 more source
The allosteric L-lactate dehydrogenases of Lactobacillus curvatus and Lactobacillus casei exist in the tetrameric from (molecular weight about 145 000) at pH 5.0--5.5 even in the absence of the effectors Mn2+ and Fru(1,6)P2 (fructose 1,6-bisphosphate ...
U. Mayr, R. Hensel, O. Kandler
semanticscholar +1 more source
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 ...
Claude Burstein, Viviane Casimiri
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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 ...
Claude Burstein, Viviane Casimiri
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The occurrence of l-lactate dehydrogenase in the inner mitochondrial compartment of pig liver
Biochemical and Biophysical Research Communications, 2017Although pig represents a model species in biomedical research including studies dealing with liver patho-physiology, some aspects of liver metabolism need to be addressed. In particular, whether and how pig mitochondria can metabolize l-lactate remains to be established.
PAVENTI, Gianluca +2 more
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