Results 301 to 310 of about 275,928 (338)
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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
openaire   +1 more source

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
openaire   +2 more sources

Co-immobilized L-lactate oxidase and L-lactate dehydrogenase on a film mounted on oxygen electrode for highly sensitive L-lactate determination

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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Enhanced stability of l -lactate dehydrogenase through immobilization engineering

Process Biochemistry, 2016
Abstract 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
openaire   +1 more source

Soybean l-(+)-lactate dehydrogenases: Purification, characterization, and resolution of subunit structure

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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[62] l(+)-Lactate dehydrogenase from Homarus americanus

1982
Publisher Summary This chapter discusses the assay method and properties of L (+)-lactate dehydrogenase isolated from Hornarus americanus. The activity of lactate dehydrogenase from the tail muscles of Homarus americanus is measured by monitoring spectrophotometrically the decrease or the increase in absorbance at 340 nm.
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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
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[60] l-Lactate dehydrogenase isozymes from sweet potato roots

1982
Publisher Summary This chapter describes the assay method and properties of L-lactate dehydrogenase isozymes isolated from sweet potato roots. Sweet potato contains two isozymes of L-lactate dehydrogenase. The isozymes are separated by a DE-52 cellulose column chromatography.
Kazuko Oˆba, Ikuzo Uritani
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L-Lactate dehydrogenase

1995
Dietmar Schomburg, Dörte Stephan
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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

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