Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
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Gene/Protein
Disease
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Target Concepts:
Gene/Protein
Disease
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Query: EC:3.1.3.9 (
glucose-6-phosphatase
)
3,081
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Extensive studies of parameters conditioning selection and high plating efficiency of epithelial liver cells at primary seeding allowed us to set up a technique for the routine culture of liver cells from rats of various ages (18 day-old pc to 7 month-old) in Ham F10 medium supplemented with 10 p. cent fetal calf serum and 10 p. cent human serum. Cultures, after several passages, or sometimes at primary seeding were free of fibroblasts. The quality of water for culture medium preparation was found to be a very important parameter. G-banding caryotype showed that cells in culture were diploid until 15-20 passages. Various metabolic pathways have been studied in primary culture and in cell lines: enzymes of the anaerobic metabolism of hexoses and metabolism of steroid hormones and xenobiotics. Activity of
glucose-6-phosphatase
was nearly lost in all cultures. Activity of
glucose-6-phosphatase
was nearly lost in all cultures.
Aldolase
showed a specific liver activity with a cleavage ratio of phosphofructoses (F-1,6-diP/F-1-P) equal to 1 or about 1 in several primary cultures and cell lines. Many metabolites arising from incubation of cell lines with 14C-labelled corticosterone, corticosterone-21-sulfate, testosterone and progesterone have been isolated and quantitated by gas liquid chromatography (GC) and mass fragmentography coupled to GC, using 14C/12C isotope ratio measurements. These metabolites indicate the presence in cultured cells of 3 alpha/beta-steroid-reductases, 4-ene steroid reductases and hydroxylases at various positions: 2 alpha, 2 beta, 6 alpha, 6 beta, 7 alpha, 17 beta and 16 alpha. These cell lines were able to activate carcinogens through the epoxide-diol pathway and are suitable for drug metabolism study.
...
PMID:[Hepatic tissue enzymes: study in cultures of rat liver epithelial cells. Control and analysis of cells by cytogenetic and mass spectrometric methods. Pharmacological applications]. 15 68
Using 4-month-old fetal bovine tissue, the properties of the tibia epiphyseal cartilage matrix vesicles, a type of endochondral ossification tissue, were compared with those from tracheal cartilage. The matrix vesicle fractions, obtained by collagenase digestion and differential centrifugation, were subjected to sucrose-density-gradient centrifugation. Alkaline phosphatase activity, protease activity, and lacatate dehydrogenase activity were assayed for the marker enzyme of the matrix vesicles. Matrix vesicles containing alkaline phosphatase, metalloprotease, and lacatate dehydrogenase were found in the tibia epiphyseal cartilage at a density of 1.11 g/ml. In surprising contrast, we also found matrix vesicle-like vesicles with a high density of 1.24 g/ml in the tracheal cartilage. These also contained alkaline phosphatase and lactate dehydrogenase, but not metalloprotease. The electrophoretic profiles of the lactate dehydrogenase isoenzymes from the matrix vesicle and matrix vesicle-like vesicles were identical with those of chondrocyte cytosolic lactate dehydrogenase.
Aldolase
, aspartate: 2-oxoglutarate aminotransferase, alanine: 2-oxoglutarate aminotransferase,
glucose-6-phosphatase
, glutamate dehydrogenase, catalase, and cytosolic enzymes except for lactate dehydrogenase were not detected in these vesicles. These results suggest the presence of a mechanism for specific uptake of cytosolic lactate dehydrogenase in both vesicles. In this study, a new type of matrix vesicles without protease was found in the tracheal cartilage, a kind of permanent cartilage, but not in the tibia epiphyseal cartilage, which is replaced by bone tissue.
...
PMID:A new type of matrix vesicles is found in fetal bovine tracheal cartilage. 1099 57
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