Membranes of rat liver peroxisomes.
Membranes of liver peroxisomes from rats fed with clofibrate were purified in a discontinuous gradient using a zonal rotor. The preparation consists of round or oval vesicles mostly devoid of nucleoids with a diameter ranging from 70-700 nm; open sheets are found very infrequently. Mitochondrial profiles as well as vesicles containing cytochemically demonstrable glucose 6-phosphatase are scarce; accordingly, glucose 6-phosphatase is nearly undetectable biochemically. Monoamine oxidase is absent in peroxisomal membranes. Cytochrome b5 is found in a concentration of 0.3 nmoles/mg protein, an order of magnitude comparable to the content of endoplasmic reticulum membranes. Reduction of this cytochrome with palmitoyl-CoA is possible only after recombination of the membranes with the soluble peroxisomal matrix fraction.
D000818:Animals; D002374:Catalase / Q000378:metabolism; D002458:Cell Fractionation; D003580:Cytochromes / Q000378:metabolism; D015786:Cytochromes b5; D005952:Glucose-6-Phosphatase / Q000378:metabolism; D006651:Histocytochemistry; D007425:Intracellular Membranes / Q000378:metabolism*; D008099:Liver / Q000378:metabolism*; D008297:Male; D008830:Microbodies / Q000378:metabolism*; D009243:NAD / Q000378:metabolism; D009940:Organoids / Q000378:metabolism*; D051381:Rats
D003580:Cytochromes; D009243:NAD; D015786:Cytochromes b5; D002374:Catalase; D005952:Glucose-6-Phosphatase