title: Enzymic and morphological studies on catalase positive particles from brown fat of cold adapted rats.
abstract: Brown adipose tissue of normal and cold-adapted adult rats has been investigated morphologically and cytochemically. In thin-sections catalase-positive particles appear as circular, oval or elongated profiles lying either as single particles or forming groups. Biochemical studies on peroxisomal enzymes show an increase of catalase activity to the tenfold amount after cold adaptation. The tissue is devoid of D-aminoacid oxidase and glycolate oxidase, while low activities of middle-chain-alpha-hydroxyacid oxidases could be detected. The catalase-positive particles were purified by differential and is lower than that of the liver peroxisomes. Enzymic investigations of the fractions render it probably that particles contain carnitine acetyltransferase, whereas they are lacking NAD-dependent glycerophosphate dehydrogenase. The pellets derived from the gradient centrifugation have been checked morphologically for purity. After performing DAB-cytochemistry for identification of the peroxidatic activity of catalase, most of the particles were shown to be structurally intact and homogeneously filled with reaction product.
mesh_terms: D002001:Adipose Tissue, Brown / Q000201:enzymology* / Q000648:ultrastructure; D000818:Animals; D001833:Body Temperature Regulation; D002332:Carnitine O-Acetyltransferase / Q000032:analysis; D002374:Catalase / Q000032:analysis*; D003080:Cold Temperature; D005993:Glycerolphosphate Dehydrogenase / Q000032:analysis; D008297:Male; D008830:Microbodies / Q000201:enzymology* / Q000648:ultrastructure; D008854:Microscopy, Electron; D009940:Organoids / Q000201:enzymology*; D010088:Oxidoreductases / Q000032:analysis; D051381:Rats; D013347:Subcellular Fractions / Q000201:enzymology
chemical_list: D010088:Oxidoreductases; D005993:Glycerolphosphate Dehydrogenase; D002374:Catalase; D002332:Carnitine O-Acetyltransferase