Results 221 to 230 of about 183,054 (259)
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Cloning, Sequence, and Expression of the L-(+) Lactate Dehydrogenase of Streptococcus bovis

Current Microbiology, 1997
The ldh gene encoding the fructose-1,6-diphosphate-dependent L-(+) lactate dehydrogenase from the ruminal bacterium Streptococcus bovis was cloned and sequenced. A genomic library of S. bovis JB1 DNA was constructed in lambda ZAP II and screened by use of a heterologous probe derived from the cloned Streptococcus mutans ldh gene.
H A, Wyckoff   +3 more
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The occurrence of l-lactate dehydrogenase in the inner mitochondrial compartment of pig liver

Biochemical and Biophysical Research Communications, 2017
Although 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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Low intensity microwave radiation as modulator of the l-lactate dehydrogenase activity

Medical & Biological Engineering & Computing, 2010
In this study, we investigated experimentally the possibility of modulating protein activity by low intensity microwaves by measuring alternations of L: -Lactate Dehydrogenase enzyme (LDH) activity. The LDH enzyme solutions were irradiated by microwaves of the selected frequencies and powers using the Transverse Electro-Magnetic (TEM) cell.
Vuk Vojisavljevic   +2 more
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Electrochemical characteristics of a carbon-based thick-film l-lactate biosensor using l-lactate dehydrogenase

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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The rates of disappearance of l-lactate dehydrogenase isoenzymes from plasma

Biochimica et Biophysica Acta (BBA) - Enzymology, 1967
1. 1. The M4 and H4 isoenzymes of lactate dehydrogenase (l-lactate: NAD+ oxidoreductase, EC 1.1.1.27) purified from sheep skeletal muscle and sheep heart, respectively, were injected intravenously into lambs, and their rates of disappearance from plasma were determined. 2. 2.
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An NAD+-independent l-lactate dehydrogenase from Rhizopus oryzae

Biochimica et Biophysica Acta (BBA) - Enzymology, 1971
Abstract 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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[57] l-Lactate (cytochrome) dehydrogenase (crystalline, yeast)

1966
Publisher 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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L(+)‐LACTATE DEHYDROGENASE IN THE HUMAN ORAL CAVITY

Annals of the New York Academy of Sciences, 1965
B, Eichel   +4 more
openaire   +2 more sources

Two NAD-independent l-lactate dehydrogenases drive l-lactate utilization in Pseudomonas aeruginosa PAO1.

Environmental microbiology reports, 2019
Pseudomonas aeruginosa often establishes a chronic infection in the airways of patients with cystic fibrosis (CF). l-Lactate is the most abundant carbon source in the CF sputum, and l-lactate utilization may be important for P. aeruginosa to survive in the lungs of CF patients.
Yujiao, Wang   +9 more
openaire   +1 more source

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