Results 321 to 330 of about 414,201 (353)
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European Journal of Biochemistry, 1970
Amino acid analyses of L-lactate dehydrogenase from baker’s yeast show that the minimum molecular weight (53000 daltons) of the protein is much lower than found in the literature (80000). This result, combined with those reported in the following papers,
C. Jacq, F. Lederer
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Amino acid analyses of L-lactate dehydrogenase from baker’s yeast show that the minimum molecular weight (53000 daltons) of the protein is much lower than found in the literature (80000). This result, combined with those reported in the following papers,
C. Jacq, F. Lederer
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Canadian Journal of Microbiology (print), 2004
The structural gene for L-lactate dehydrogenase (LDH) (EC.1.1.1.27) from Clostridium thermocellum 27405 was cloned in Escherichia coli by screening the Lambda Zap II phage library of C. thermocellum genomic DNA.
M. Ozkan +3 more
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The structural gene for L-lactate dehydrogenase (LDH) (EC.1.1.1.27) from Clostridium thermocellum 27405 was cloned in Escherichia coli by screening the Lambda Zap II phage library of C. thermocellum genomic DNA.
M. Ozkan +3 more
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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 ...
Hak-Sung Kim, Hyun C. Yoon
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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 ...
Hak-Sung Kim, Hyun C. Yoon
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Cloning studies on the gene coding for l-(+)-lactate dehydrogenase of Plasmodium falciparum
Molecular and Biochemical Parasitology, 1985We show that the L-(+)-lactate dehydrogenase (EC 1.1.1.27;L-lactate: NAD+-oxidoreductase) of Plasmodium falciparum (LDH-P) is encoded in the parasite genome. A monoclonal antibody (McAb 7.2) has been shown to bind the LDH-P subunit which has an apparent molecular mass of 35 kDa.
Simmons, David Ll +4 more
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Presence of an l(+)-lactate dehydrogenase in cells of Lactobacillus delbrueckii ssp. bulgaricus
Biochimie, 1989Lactobacillus delbrueckii ssp. bulgaricus ATCC 11842 was cultured in a chemostat and growth conditions were varied as required. Synthesis of L(+)-lactate was observed in all cases as well as activity of L(+)-lactate dehydrogenase in cell-free extracts. This enzyme was responsible for the formation of the L(+) isomer of lactate, since a lactate racemase
Aida Pesce de Ruiz Holgado +3 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.
L.A. Burgoyne, R.H. Symons
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Molecular Biotechnology, 2016
Theileria annulata is a parasite that causes theileriosis in cattle. Reports about drug resistance made essential to develop new drug. LDH of Theileria schizonts is the vital enzyme for its anaerobic metabolism. TaLDH gene was first cloned into pGEM-T cloning vector with two introns in our previous study. Here we report cloning of TaLDH without introns
Nural, Belma +6 more
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Theileria annulata is a parasite that causes theileriosis in cattle. Reports about drug resistance made essential to develop new drug. LDH of Theileria schizonts is the vital enzyme for its anaerobic metabolism. TaLDH gene was first cloned into pGEM-T cloning vector with two introns in our previous study. Here we report cloning of TaLDH without introns
Nural, Belma +6 more
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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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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 ...
A. Fontanell +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 ...
A. Fontanell +3 more
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Cloning and characterization of a l-lactate dehydrogenase gene from Ruminococcaceae bacterium CPB6
World Journal of Microbiology & Biotechnology, 2020Qingzhuoma Yang +4 more
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