Results 161 to 170 of about 10,826 (186)
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Biochemistry and Cell Biology, 1992
We used the N-terminal amino acid sequence of dihydrolipoamide dehydrogenase from Haloferax volcanii, to design and synthesize two oligonucleotide probes that were used to identify and clone a 4.3 kilobase pair (kbp) fragment from MboI restriction endonuclease digestion of Hf. volcanii genomic DNA.
N N, Vettakkorumakankav, K J, Stevenson
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We used the N-terminal amino acid sequence of dihydrolipoamide dehydrogenase from Haloferax volcanii, to design and synthesize two oligonucleotide probes that were used to identify and clone a 4.3 kilobase pair (kbp) fragment from MboI restriction endonuclease digestion of Hf. volcanii genomic DNA.
N N, Vettakkorumakankav, K J, Stevenson
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Refolding of the human dihydrolipoamide dehydrogenase
Biochemical Engineering Journal, 2009Abstract A refolding procedure was optimized for human dihydrolipoamide dehydrogenase (LADH) that can serve as a complementary method to isolation protocols for cytosolic or periplasmic expression of the enzyme. The reported procedure is especially useful if part of the protein is precipitated into inclusion bodies during expression and higher ...
Attila Ambrus +2 more
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Elevated plasma citrulline: look for dihydrolipoamide dehydrogenase deficiency
European Journal of Pediatrics, 2013The E3 subunit of the pyruvate dehydrogenase complex (dihydrolipoamide dehydrogenase/dihydrolipoyl dehydrogenase/DLD/lipoamide dehydrogenase/LAD), is a mitochondrial matrix enzyme and also a part of the branched-chain ketoacid dehydrogenase and alpha-ketoglutarate dehydrogenase complexes.
Ruby, Haviv +4 more
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Journal of Molecular Recognition, 2021
AbstractDihydrolipoamide dehydrogenase (DLDH) is a homodimeric flavin‐dependent enzyme that catalyzes the NAD+‐dependent oxidation of dihydrolipoamide. The enzyme is part of several multi‐enzyme complexes such as the Pyruvate Dehydrogenase system that transforms pyruvate into acetyl‐co‐A.
Gideon Fleminger, Avraham Dayan
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AbstractDihydrolipoamide dehydrogenase (DLDH) is a homodimeric flavin‐dependent enzyme that catalyzes the NAD+‐dependent oxidation of dihydrolipoamide. The enzyme is part of several multi‐enzyme complexes such as the Pyruvate Dehydrogenase system that transforms pyruvate into acetyl‐co‐A.
Gideon Fleminger, Avraham Dayan
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Roles of dihydrolipoamide dehydrogenase Lpd1 in Candida albicans filamentation
Fungal Genetics and Biology, 2010Acetyl coenzyme A, a key intermediate of the mitochondrial carbon metabolism, is formed by the mitochondrial pyruvate dehydrogenase complex (PDC). The dihydrolipoamide dehydrogenase Lpd1 is a catalytic component of PDC. Lpd1 has been recovered during 2D-PAGE screening for the hypha-specific proteins in Candida albicans.
Seung-Yeop, Kim, Jinmi, Kim
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Rat liver mitochondria contain two immunologically distinct dihydrolipoamide dehydrogenases
Archives of Biochemistry and Biophysics, 1987We have raised antisera against dihydrolipoamide dehydrogenase. One antigen was isolated from purified bovine kidney pyruvate dehydrogenase complex (PDC). The other antigen was a commercial preparation of porcine heart dihydrolipoamide dehydrogenase (E3) which did not first involve purification of the alpha-keto acid dehydrogenase complex(es).
D J, Carothers +3 more
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Dihydrolipoamide dehydrogenase: activity assays.
Methods in enzymology, 1995We have described the most commonly used assay procedures determination of the DHLipDH activities from prokaryotic and eukaryotic cells. We have also described the procedures for the preparation of tissue extracts to determine the enzymatic activity.
M S, Patel +2 more
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Hamster sperm capacitation: role of pyruvate dehydrogenase A and dihydrolipoamide dehydrogenase.
Biology of reproduction, 2008Recently, we demonstrated that pyruvate dehydrogenase A2 (PDHA2) is tyrosine phosphorylated in capacitated hamster spermatozoa. In this report, using bromopyruvate (BP), an inhibitor of PDHA, we demonstrated that hamster sperm hyperactivation was blocked regardless of whether PDHA was inhibited prior to or after the onset of hyperactivation, but the ...
Vivek, Kumar +2 more
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Dihydrolipoamide dehydrogenase moonlighting activity as a
Abstract Dihydrolipoamide dehydrogenase (DLDH) is a mitochondrial enzyme that comprises an essential component of the pyruvate dehydrogenase complex. Lines of evidence have shown that many dehydrogenases possess unrelated actions known as moonlightings in addition to their oxidoreductase activity. As part of these
Avraham Dayan +4 more
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Protein Expression and Purification, 2003
Plasmids were constructed for overexpression of the Escherichia coli dihydrolipoamide acetyltransferase (1-lip E2, with a single hybrid lipoyl domain per subunit) and dihydrolipoamide dehydrogenase (E3). A purification protocol is presented that yields homogeneous recombinant 1-lip E2 and E3 proteins.
Wen, Wei +3 more
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Plasmids were constructed for overexpression of the Escherichia coli dihydrolipoamide acetyltransferase (1-lip E2, with a single hybrid lipoyl domain per subunit) and dihydrolipoamide dehydrogenase (E3). A purification protocol is presented that yields homogeneous recombinant 1-lip E2 and E3 proteins.
Wen, Wei +3 more
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