Results 281 to 290 of about 312,266 (316)

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 ...
Claude Burstein, Viviane Casimiri
openaire   +2 more sources

Factors affecting the quaternary structure of the allosteric L-lactate dehydrogenase from Lactobacillus casei and Lactobacillus curvatus as investigated by hybridization and ultracentrifugation.

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 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, PIZZUTO, Roberto, PASSARELLA, Salvatore   +2 more
openaire   +4 more sources

Molecular weight and quaternary structure of yeast L-lactate dehydrogenase (cytochrome b2). 1. Minimum molecular weight from amino acid analyses.

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
semanticscholar   +1 more source

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 ...
Hak-Sung Kim, Hyun C. Yoon
openaire   +2 more sources

Cloning and expression of the Clostridium thermocellum L-lactate dehydrogenase gene in Escherichia coli and enzyme characterization.

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, E. Yilmaz, L. Lynd, G. Ozcengiz   +3 more
semanticscholar   +1 more source

Cloning studies on the gene coding for l-(+)-lactate dehydrogenase of Plasmodium falciparum

Molecular and Biochemical Parasitology, 1985
We 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, Hyde, John E., Mackay, Martin, Goman, Mike, Scaife, John   +4 more
openaire   +3 more sources

Presence of an l(+)-lactate dehydrogenase in cells of Lactobacillus delbrueckii ssp. bulgaricus

Biochimie, 1989
Lactobacillus 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, Guillermo Oliver, Alicia Ragout, Faustino Siñeriz   +3 more
openaire   +3 more sources

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   +3 more sources

Biochemical and in silico Characterization of Recombinant L-Lactate Dehydrogenase of Theileria annulata

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, Mutlu, Özal, Turgut-Balık, Dilek, Topuzogulları, Murat, Erdemir, Ayşegül, Danıs, Özkan, Yakarsonmez, Sinem   +6 more
openaire   +4 more sources