title: Characterization of peroxisomes in Chinese hamster ovary cells in culture.
abstract: In order to explore the potential value of Chinese hamster ovary (CHO) cells for the isolation of peroxisomal mutants defective in the peroxisomal fatty acid oxidation system, some characteristics of their peroxisomes were studied. Catalase was detected biochemically and histochemically in peroxisome-like particles in cells or in subcellular fractions prepared by differential centrifugation or isopyknic equilibrium in Percoll or Metrizamide with catalase in the high density fractions of the isopyknic equilibrium gradients. By oxidation system, exhibited an unusually high specific activity, 2.46 +/- 1.09 mU/mg protein, in CHO cell homogenates, a value comparable to that of rat liver. This enzyme copurifies with catalase in the high density fractions of the isopycnic equilibrium gradients. By analogy with other cell types and from the ultrastructural analysis, it is concluded that these enzymes are contained in peroxisomes. These findings support the value of CHO cells for studies of peroxisomal function and organization.
mesh_terms: D042962:Acyl-CoA Oxidase; D000818:Animals; D002374:Catalase / Q000378:metabolism*; D002458:Cell Fractionation; D002460:Cell Line; D002499:Centrifugation, Density Gradient; D006224:Cricetinae; D003412:Cricetulus; D005260:Female; D008830:Microbodies / Q000201:enzymology* / Q000648:ultrastructure; D008854:Microscopy, Electron; D010053:Ovary; D010088:Oxidoreductases / Q000378:metabolism*; D013347:Subcellular Fractions / Q000201:enzymology
chemical_list: D010088:Oxidoreductases; D002374:Catalase; D042962:Acyl-CoA Oxidase