Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.6.99.3 (diaphorase)
 5,903 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Maruyama, Yoshiharu (Cornell University, Ithaca, N.Y.) and Martin Alexander. Localization of enzymes in the mycelium and microconidia of Fusarium oxysporum. J. Bacteriol. 84:307-312. 1962-Extracts prepared from mycelium and microconidia of Fusarium oxysporum f. cubense were fractionated into a soluble and four particulate fractions by differential centrifugation, and the distribution of several enzymes in the isolated cell constituents was examined. Succinic dehydrogenase, cytochrome oxidase, and a large amount of the reduced diphosphopyridine nucleotide (DPNH) cytochrome c reductase and reduced triphosphopyridine nucleotide cytochrome c reductase were associated with one of the particulate fractions prepared from the hyphae; fumarase and DPNH oxidase activities were largely found in the soluble and in a second particulate fraction. The highest recovery and concentration of diphosphopyridine nucleotidase was observed to be bound to a third type of hyphal granule. Aldolase, aconitase, glucose-6-phosphatase, and uricase were recovered entirely with the soluble mycelium constituents. Similar enzyme-distribution patterns were observed in microconidia. Several enzymatic activities of the mycelial extracts were compared with those in the extracts of microconidia.
 ...
PMID:Localization of enzymes in the mycelium and microconidia of Fusarium oxysporum. 1447 Jun 62

Although protein carbonyl formation is an index of oxidative stress in skeletal muscles, the exact proteins, which undergo oxidation in these muscles, remain unknown. We used 2D electrophoresis, immunoblotting, and mass spectrometry to identify carbonylated proteins in the diaphragm in septic animals. Rats were injected with saline (control) or Escherichia coli lipopolysaccharides (LPS) and killed after various intervals. Diaphragm protein carbonylation increased significantly and peaked 12 h after LPS injection, and it was localized both inside muscle fibers and in blood vessels supplying muscle fibers. Aldolase A, glyceraldehyde 3-phosphate dehydrogenase, enolase 3beta, mitochondrial and cytosolic creatine kinases, alpha-actin, carbonic anyhdrase III, and ubiquinol-cytochrome c reductase were all carbonylated in septic rat diaphragms. In addition, we found significant negative correlations between the intensity of carbonylation and creatine kinase and aldolase activities. We conclude that glycolysis, ATP production, CO2 hydration, and contractile proteins are targeted by oxygen radicals inside the diaphragm during sepsis.
 ...
PMID:Protein carbonyl formation in the diaphragm. 1547 39