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  • Cytochromec oxidase  (1)
  • Dimorphism  (1)
  • 1985-1989  (2)
  • 1965-1969
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 144 (1986), S. 124-130 
    ISSN: 1432-072X
    Keywords: Dimorphism ; Yarrowia lipolytica ; Cell wall composition
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The cell walls of the yeast and mycelial forms of Yarrowia lipolytica were isolated and purified. Electron microscopy studies showed no differences between both types of cell walls. Chemical analysis revealed that the yeast cell wall contained 70% neutral carbohydrate, 7% amino sugars, 15% protein, 5% lipids and 0.8% phosphorus. Mycelial cell walls contained 70% carbohydrate, 14% aminosugars, 6% protein, 5% lipids and 0.6% phosphorus. Three polysaccharides: β-glucan, mannan and chitin were detected. Proteins were solubilized from both cell wall fractions and separated by polyacrylamide gel electrophoresis. About 50 protein bands were detected, four of them corresponding to glycoproteins. The cell walls of the yeast and mycelial forms of Y. lipolytica were qualitatively similar and only quantitative differences were found.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-6881
    Keywords: Cytochromec oxidase ; respiratory chain ; complex IV ; mitochondrial myopathies ; mitochondrial encephalomyopathies ; maternal inheritance ; isozymes ; Leigh syndrome ; MERRF (myoclonus epilepsy with ragged-red fibers)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract Defects of cytochromec oxidase (COX) show remarkable clinical, biochemical, and genetic heterogeneity. Clinically, there are two main groups of disorders, one dominated by muscle involvement, the other by brain dysfunction. Biochemically, the enzyme defect may be confined to one or a few tissues (reflecting the existence of tissue-specific isozymes) or affect all tissues. Immunologically reactive enzyme protein is decreased in some forms of COX deficiency but not in others. Because COX is encoded both by nuclear and by mitochondrial genes, COX deficiencies may be due to mutations of either genome and may offer useful models to study the communication between nuclei and mitochondria. We have isolated full-length cDNA clones encoding human COX subunits IV, Vb, and VIII and a partial-length clone for subunit Va. These clones are being used as probes to analyze the DNA and RNA of patients with COX deficiency.
    Type of Medium: Electronic Resource
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