digitonin and Kidney-Diseases

digitonin has been researched along with Kidney-Diseases* in 1 studies

Other Studies

1 other study(ies) available for digitonin and Kidney-Diseases

Article	Year
Activity of peroxisomal enzymes and intracellular distribution of catalase in Zellweger syndrome. Biochemical and biophysical research communications, 1984, Sep-28, Volume: 123, Issue:3 The activity of peroxisomal enzymes was studied in human liver and cultured human skin fibroblasts in relation to the finding (Goldfischer, S. et al. (1973) Science 182, 62-64) that morphologically distinct peroxisomes are not detectable in patients with the cerebro-hepato-renal (Zellweger) syndrome. In homogenates of liver from the patients, dihydroxyacetone phosphate acyltransferase, a membrane-bound peroxisomal enzyme, is deficient (Schutgens, R.B.H., et al. (1984) Biochem. Biophys. Res. Commun. 120, 179-184). In contrast, there is no deficiency of the soluble peroxisomal matrix enzymes catalase, L-alpha-hydroxyacid oxidase and E-aminoacid oxidase. Catalase is also not deficient in homogenates of cultured skin fibroblasts from the patients. The results of digitonin titration experiments showed that in control fibroblasts at least 70% of the catalase activity is present in subcellular particles distinct from mitochondria or lysosomes. In contrast, all of the catalase activity in fibroblasts from Zellweger patients is found in the same compartment as the cytosolic marker enzyme lactate dehydrogenase. Topics: Acyltransferases; Alcohol Oxidoreductases; Brain Diseases; Catalase; Cells, Cultured; D-Amino-Acid Oxidase; Digitonin; Fibroblasts; Humans; Kidney Diseases; Kinetics; Liver Diseases; Microbodies; Skin; Syndrome	1984

Article

Year

Activity of peroxisomal enzymes and intracellular distribution of catalase in Zellweger syndrome.

Biochemical and biophysical research communications, 1984, Sep-28, Volume: 123, Issue:3

The activity of peroxisomal enzymes was studied in human liver and cultured human skin fibroblasts in relation to the finding (Goldfischer, S. et al. (1973) Science 182, 62-64) that morphologically distinct peroxisomes are not detectable in patients with the cerebro-hepato-renal (Zellweger) syndrome. In homogenates of liver from the patients, dihydroxyacetone phosphate acyltransferase, a membrane-bound peroxisomal enzyme, is deficient (Schutgens, R.B.H., et al. (1984) Biochem. Biophys. Res. Commun. 120, 179-184). In contrast, there is no deficiency of the soluble peroxisomal matrix enzymes catalase, L-alpha-hydroxyacid oxidase and E-aminoacid oxidase. Catalase is also not deficient in homogenates of cultured skin fibroblasts from the patients. The results of digitonin titration experiments showed that in control fibroblasts at least 70% of the catalase activity is present in subcellular particles distinct from mitochondria or lysosomes. In contrast, all of the catalase activity in fibroblasts from Zellweger patients is found in the same compartment as the cytosolic marker enzyme lactate dehydrogenase.

Topics: Acyltransferases; Alcohol Oxidoreductases; Brain Diseases; Catalase; Cells, Cultured; D-Amino-Acid Oxidase; Digitonin; Fibroblasts; Humans; Kidney Diseases; Kinetics; Liver Diseases; Microbodies; Skin; Syndrome

1984