Hypoxic pregnancy promotes fibrosis and increases stress metabolites in the ovine fetal liver. [PDF]
McGuckin MM+8 more
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PDH Inhibition in <i>Drosophila</i> Ameliorates Sensory Dysfunction Induced by Vincristine Treatment in the Chemotherapy-Induced Peripheral Neuropathy Models. [PDF]
Song H, Kim S, Han JE, Kang KH, Koh H.
europepmc +1 more source
Integration of Transcriptomics and Metabolomics Reveals Mechanisms of High-Temperature Stress Tolerance in the Hepatopancreas of <i>Penaeus monodon</i>. [PDF]
Liu L+9 more
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Molecular Imaging: Unveiling Metabolic Abnormalities in Pancreatic Cancer. [PDF]
Wang H, Gui Y, Lv K.
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Lactobacillus plantarum: From Application to Protein Expression (Lactobacillus plantarum: Sovellutuksista proteiinien ilmentymiseen) [PDF]
Plumed-Ferrer, Carme
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One-Step Purification of the Recombinant Catalytic Subunit of Pyruvate Dehydrogenase Phosphatase
A facile one-step affinity chromatographic purification of the recombinant catalytic subunit (PDPc) of bovine pyruvate dehydrogenase phosphatase (PDP) to near homogeneity is described. PDPc binds in the presence of Ca(2+) to the inner lipoyl domain (L2) of the dihydrolipoamide acetyltransferase component (E2) of the mammalian pyruvate dehydrogenase ...
Wahn Soo Choi+4 more
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[Pyruvate dehydrogenase (lipoamide)]-phosphatase
Dietmar Schomburg, Margit Salzmann
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Inhibition of pyruvate dehydrogenase and pyruvate dehydrogenase phosphate phosphatase by glyoxylate
Bioorganic Chemistry, 1985Abstract The overall reaction catalyzed by the pyruvate dehydrogenase complex from rat epididymal fat tissue is inhibited by glyoxylate at concentrations greater than 10 μ m . The inhibition is competitive with respect to pyruvate; Ki was found to be 80 μ m .
Gordon A. Hamilton, Susan M. Beatty
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Stimulation of pyruvate dehydrogenase phosphatase activity by polyamines
Biochemical and Biophysical Research Communications, 1984Pyruvate dehydrogenase phosphatase requires Mg2+ or Mn2+, and its activity in the presence of Mg2+ is markedly stimulated by Ca2+. At saturating Mg2+ and Ca2+ concentrations, the polyamines spermine, spermidine and putrescine stimulated the activity of pyruvate dehydrogenase phosphatase 1.5- to 3-fold. Spermine was the most active of the polyamines. At
Lester J. Reed+2 more
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