[42] Glucose-6-phosphate dehydrogenase 6-phosphogluconic dehydrogenase

Kornberg, Arthur; Horecker, B.L.; Smyrniotis, P.Z.

doi:10.1016/0076-6879(55)01046-x

Cited by 556 publications

(61 citation statements)

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“…Glutathione peroxidase (GP x ) activity (Paglia and Valentine, 1967), Glucose-6-phosphate dehydrogenase (G6PDH) activity (Kornberg et al, 1955) and catalase activity (CAT) (Beulter, 1975) were determined in fresh blood hemolysates. Liver glycogen, total protein, RNA and DNA concentrations were also assessed in the diluted whole liver homogenates (Dubois et al, 1956;Markwell et al, 1978;Dische and Schwartz, 1954;and Dische, 1957, respectively).…”

Section: Biochemical Assaysmentioning

confidence: 99%

Antitumor Activities of Iodoacetate and Dimethylsulphoxide Against Solid Ehrlich Carcinoma Growth in Mice

Fahim

Esmat²,

Mady³

et al. 2003

Biol. Res.

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Treatment of tumor-bearing mice with LD 12.5 values of iodoacetate; IAA (1.84 mg/100g b.w.) and/or dimethylsulphoxide; DMSO (350 mg/ 100g b.w.) significantly increased the cumulative mean survival time and percentage of survivors and reduced the mean tumor weight, compared to tumor-bearing controls, however, a more pronounced effect is recorded in the combined treatment. Also, an increase in the life span (ILS%) and tumor growth inhibition ratio (T/C%) are reported and amounted to 145.78 and 43.80%, 195.54 and 61.30% and 220.77 and 78.40% in IAA, DMSO and combined-treated groups, respectively. Results obtained from biochemical studies reveal that a single IAA treatment of tumor-bearing mice significantly increased the levels of plasma lactate dehydrogenase (LDH) activity, while it also significantly decreased the levels of plasma glucose and liver total protein, RNA and DNA, compared to normal controls. On the other hand, a single DMSO treatment significantly elevated the activities of blood antioxidant enzymes, i.e. glutathione peroxidase (GP x ) and glucose-6-phosphate dehydrogenase (G6PDH) and decreased the liver RNA and DNA levels. Combined treatment increased significantly the levels of plasma LDH and erythrocytes G6PDH activities, as well as liver glycogen, and in contrast it decreased the levels of liver total protein, RNA and DNA, compared to normal controls.

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Section: Biochemical Assaysmentioning

confidence: 99%

Antitumor Activities of Iodoacetate and Dimethylsulphoxide Against Solid Ehrlich Carcinoma Growth in Mice

Fahim

Esmat²,

Mady³

et al. 2003

Biol. Res.

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“…Glucose-6-phosphate dehydrogenase was assayed by measuring the rate of increase in absorbance of NADPH at 25 "C [31]. Malate dehydrogenase [32], lactate dehydrogenase [33] and glutamate dehydrogenase [34] were assayed by measuring the rate of decrease in absorbance of NADH at 25 "C. Glyceraldehyde-3-phosphate dehydrogenase was assayed by measuring the coupled reaction with phosphoglycerate kinase 1351.…”

Section: Preparation and Assay O J Substrate Enzymesmentioning

confidence: 99%

Crystallization and Properties of Cathepsin B from Rat Liver

1979

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Cathepsin B from rat liver was purified to apparent homogeneity by cell-fractionation, freezing and thawing, acetone treatment, gel filtration, DEAE-Sephadex and CM-Sephadex column chromatography, and was crystallized. The purified enzyme formed spindle-shaped crystals and its homogeneity was proved by disc gel electrophoresis in the presence of sodium dodecyl sulfate and by ultracentrifugical analysis.Its ~2 0 ,~ value was 2.8 S and its relative molecular mass was calculated to be 22 500 (k 900) by sedimentation equilibrium analysis. Crystalline cathepsin B was shown to consist of four isozymes with isoelectric points between pH 4.9 and 5.3, the main isozyme having an isoelectric point of pH 5.0. The enzyme was irreversibly inactivated by exposure to weak alkali. The pH optimum was 6.0 with a-N-benzoyl-~~-arginine-4-nitroanilide as substrate. Amino acid analysis showed that the enzyme contained hexosamine, glucosamine and galactosamine. Cathepsin B inactivated aldolase, glucokinase, apo-ornithine aminotransferase, and apo-cystathionase, but the rates of inactivation of glucokinase, apo-ornithine aminotransferase, and apocystathionase were lower than that of aldolase. Studies by polyacrylamide gel electrophoresis in the presence and absence of sodium dodecyl sulfate showed that cathepsin B degraded apo-ornithine aminotransferase to two polypeptide chains differing in relative molecular mass and electrophoretic mobility.Inhibitors of so-called cathepsin B reduce protein degradation in various experimental systems. This has been demonstrated with leupeptin in a system in vitro [l] and in tissue culture [2] and with chloroquine in tissue culture [3]. Therefore, it is thought that cathepsin B is important in intracellular protein degradation. Cathepsin B has been found in various mammalian tissues and its purification has been attempted by many workers. The preparation of cathepsin B of Greenbaum and Fruton [4] was demonstrated by Otto

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“…and assayed by the method of RACKER (12). Glucose-6-phosphate dehyrogenase was prepared from brewer's yeast according to the method of KoRNBERG et al (13). Alcohol dehydro-VOL.…”

Section: Measurementmentioning

confidence: 99%