Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.3.9 (glucose-6-phosphatase)
 3,081 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Peroxisome proliferation has been induced with 2-methyl-2-(p-[1,2,3,4-tetrahydro-1-naphthyl]-phenoxy)-propionic acid (Su-13437). DNA, protein, cytochrome oxidase, glucose-6-phosphatase, and acid phosphatase concentrations remain almost constant. Peroxisomal enzyme activities change to approximately 165%, 50%, 30%, and 0% of the controls for catalase, urate oxidase, L-alpha-hydroxy acid oxidase, and D-amino acid oxidase, respectively. For catalase the change results from a decrease in particle-bound activity and a fivefold increase in soluble activity. The average diameter of peroxisome sections is 0.58 +/- 0.15 mum in controls and 0.73 +/- 0.25 mum after treatment. Therefore, the measured peroxisomal enzymes are highly diluted in proliferated particles. After tissue fractionation, approximately one-half of the normal peroxisomes and all proliferated peroxisomes show matric extraction with ghost formation, but no change in size. In homogenates submitted to mechanical stress, proliferated peroxisomes do not reveal increased fragility; unexpectedly, Su-13437 stabilizes lysosomes. Our results suggest that matrix extraction and increased soluble enzyme activities result from transmembrane passage of peroxisomal proteins. The changes in concentration of peroxisomal oxidases and soluble catalase after Su-13437 allow the calculation of their half-lives. These are the same as those found for total catalase, in normal and treated rats, after allyl isopropyl acetamide: about 1.3 days, a result compatible with peroxisome degradation by autophagy. A sequential increase in liver RNA concentration, [14C]leucine incorporation into DOC-soluble proteins and into immunoprecipitable catalase, and an increase in liver size and peroxisomal volume per gram liver, characterize the trophic effect of the drug used. In males, Su-13437 is more active than CPIB, another peroxisome proliferation-inducing drug; in females, only Su-13437 is active.
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PMID:Structure, composition, physical properties, and turnover of proliferated peroxisomes. A study of the trophic effects of Su-13437 on rat liver. 0 Apr 6

The peroxisomal core from the liver of rats was purified 450-fold as a marker of urate oxidase [EC 1.7.3.3.] activity. This preparation has a high specific activity of urate oxidase but not of other peroxisomal enzymes: D-amino acid oxidase [EC 1.4.3.3.], L-alpha-hydroxy acid oxidase [EC 1.1.3.15], or catalase [EC 1.11.1.6]. No activity of marker enzymes for other subcellular particles; cytochrome c oxidase [EC1.9.3.1] (mitochondria), acid phosphatase [EC 3.1.3.2] (lysosomes), or glucose-6-phosphatase [EC 3.1.3.9] (microsomes), was detected in this preparation. The core obtained showed a single protein band in sodium dodecyl sulfate-polyacrylamide gel electrophoresis and the position of the band was found to correspond to a molecular weight 35,000. When the peroxisomal core was subjected to treatment at various pH's with 0.1 M carbonate buffer, urate oxidase was almost completely solubulized at pH 11.0, although approximately 35% of the core protein still remained in the pellet After solubilization of the core at pH 11.0, the specific activity of urate oxidase in the supernatant increased about 1.6 times; the density of the insoluble protein remaining in the pellet was identical with the that of the original core on sucrose density gradient centrifugation.
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PMID:Studies on peroxisomes. VI. Relationship between the peroxisomal core and urate oxidase. 0 33

The protein content and activity of enzymatic markers of cell organelles: succinate dehydrogenase, glucose-6-phosphatase, uricase, acid phosphatase, 5'-nucleotidase and alkaline phosphatase were assayed in the homogenate and the supernatant (after two-hour centrifugation at 140,000 X g) of the liver and intestinal epithelium in rabbits irradiated with a single dose of 550 rads of gamma rays. The determinations were carried out on 1,3,6,9,15 and 30 days after irradiation for experimental and control animals. After gamma irradiation the following alterations were found: 1) increase in protein content (marked between 3-6 days), 2) remarkable rise of alkaline phosphatase activity (during the entire period of study), 3) elevation of 5'-nucleotidase activity (only in the intestinal epithelium), 4) marked reduction of succinate dehydrogenase and uricase activity (on the first day of study), 5) moderate decrease of glucose-6-phosphatase activity (mainly on the third day). Apart from a slight decline in the activity of acid phosphatase in the homogenate of intestinal epithelium, on the third day there practically were no changes in the activity of this enzyme either in the supernatant of intestinal epithelium or in the liver tissue.
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PMID:Effect of gamma radiation on the enzymatic activity of cell organelles of liver and epithelium of small intestine in rabbits. 123 88

A preparative method for the isolation of peroxisomes from the liver of normal, untreated rats is described. The peroxisome-enriched "light mitochondrial" fraction is layered on a 30% Nycodenz (5-[N-2,3-dihydroxypropylacetamido]-2,4,6-triiodo-N,N'-bis[2, 3-dihydroxypropyl]isophthalamide) solution containing 1 mM tetrasodium EDTA and then centrifuged in an angular rotor for 1 h at 130,000gavg. Peroxisomes are sedimented to the bottom leaving other organelles at the top of the tube. On the basis of morphological and biochemical studies, it is found that the peroxisomes (marker-enzymes catalase and urate oxidase) obtained in this method are not contaminated with lysosomes (marker-enzyme acid phosphatase) and contained very few mitochondria (marker-enzyme succinate-cytochrome c reductase) and microsomal vesicles (marker-enzyme glucose-6-phosphatase).
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PMID:A rapid method for the isolation of peroxisomes from rat liver. 381 96

Enzymatic activities associated with Golgi apparatus-, endoplasmic reticulum-, plasma membrane-, mitochondria-, and microbody-rich cell fractions isolated from rat liver were determined and used as a basis for estimating fraction purity. Succinic dehydrogenase and cytochrome oxidase (mitochondria) activities were low in the Golgi apparatus-rich fraction. On the basis of glucose-6-phosphatase (endoplasmic reticulum) and 5'-nucleotidase (plasma membrane) activities, the Golgi apparatus-rich fraction obtained directly from sucrose gradients was estimated to contain no more than 10% endoplasmic reticulum- and 11% plasma membrane-derived material. Total protein contribution of endoplasmic reticulum, mitochondria, plasma membrane, microbodies (uric acid oxidase), and lysosomes (acid phosphatase) to the Golgi apparatus-rich fraction was estimated to be no more than 20-30% and decreased to less than 10% with further washing. The results show that purified Golgi apparatus fractions isolated routinely may exceed 80% Golgi apparatus-derived material. Nucleoside di- and triphosphatase activities were enriched 2-3-fold in the Golgi apparatus fraction relative to the total homogenate, and of a total of more than 25 enzyme-substrate combinations reported, only thiamine pyrophosphatase showed a significantly greater enrichment.
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PMID:Isolation of a Golgi apparatus-rich fraction from rat liver. II. Enzymatic characterization and comparison with other cell fractions. 431 70

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.
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PMID:Localization of enzymes in the mycelium and microconidia of Fusarium oxysporum. 1447 Jun 62