Association of monoamine oxidase and malate dehydrogenase with liver peroxisomes of genetically obese (ob/ob and db/db) mice

V.M. Mann, V.U. Nwosu, A. Silcox, Carolyn Jones, K. Burdett, M.J. Connock

    Research output: Contribution to journalArticlepeer-review


    1. 1. Liver post-nuclear supernatants (PNS) from genetically obese (ob/ob and db/db), lean (+/?), and albino mice were fractionated by dual centrifugation in B-XIV zonal rotors and subcellular fractions were analysed by marker-enzyme estimation and by electron microscopy. 2. 2. Rate-dependent banding of PNS yielded a peroxisome-enriched region (PER) well-separated from mitochondria. 3. 3. Density-dependent banding of PER in ob/ob and db/db mice only, yielded purified peroxisomes which were associated with malate dehydrogenase (cytosolic) and monoamine oxidase. 4. 4. Markers for the mitochondrial matrix, intermembrane space and inner membrane compartments were absent from the peroxisomes. 5. 5. The experimental results are interpreted as indicating that peroxisomes of genetically obese mice are either altered so that protein import or so that their attachment to mitochondria is more extensive. © 1992.
    Original languageUndefined
    Pages (from-to)561-571
    Number of pages11
    JournalComparative Biochemistry and Physiology -- Part B: Biochemistry and
    Issue number3
    Publication statusPublished - 1992


    • amine oxidase (flavin containing)
    • malate dehydrogenase, animal model
    • animal tissue
    • article
    • genetic disorder
    • liver
    • mouse
    • nonhuman
    • obesity
    • peroxisome
    • priority journal, Animal
    • Biological Markers
    • Cell Fractionation
    • Centrifugation, Density Gradient
    • Female
    • Liver
    • Malate Dehydrogenase
    • Male
    • Mice
    • Mice, Obese
    • Microbodies
    • Microscopy, Electron
    • Monoamine Oxidase
    • Obesity, Animalia

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