Purification of guinea pig small intestinal peroxisomes and the subcellular localization of glucose-6-phosphate dehydrogenase

P.S. Tappia, Carolyn Jones, M.J. Connock

    Research output: Contribution to journalArticlepeer-review


    A method for the isolation of highly purified peroxisomes from guinea pig small intestine was developed. This two-stage process involved a rate-dependent banding of a light-mitochondria lambda-fraction followed by a density-dependent banding of the catalase enriched fractions obtained from the first step, using a horizontal rotor. Furthermore, the subcellular localization of glucose-6-phosphate dehydrogenase (NADP+-dependent) activity in guinea pig small intestine was examined. Analysis of density-gradient fractions indicated that approximately 3-4% of the cellular NADP+-dependent glucose-6-phosphate dehydrogenase activity is associated with peroxisomal fractions and that it is localized to the matrix of peroxisomes. It is therefore suggested that a peroxisomal source of NADPH may be utilized by enzyme systems that use NADPH specifically as a reductant.
    Original languageUndefined
    Pages (from-to)13-20
    Number of pages8
    JournalMolecular and Cellular Biochemistry
    Issue number1-2
    Publication statusPublished - 1998


    • catalase
    • glucose 6 phosphate dehydrogenase
    • nicotinamide adenine dinucleotide phosphate, animal tissue
    • article
    • cellular distribution
    • density gradient centrifugation
    • enzyme activity
    • enzyme localization
    • guinea pig
    • male
    • nonhuman
    • peroxisome
    • purification
    • small intestine
    • technique, Animals
    • Biological Markers
    • Cell Fractionation
    • Centrifugation, Density Gradient
    • Glucosephosphate Dehydrogenase
    • Guinea Pigs
    • Intestine, Small
    • Male
    • Metrizamide
    • Microbodies
    • Microscopy, Electron
    • NADP
    • Octoxynol, Animalia
    • Cavia porcellus
    • Sus scrofa

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