Cytochemical localization of peroxidase activity in the mitochondria of Hymenolepis diminuta.
A cytochemical study of mitochondria of Hymenolepis diminuta indicates the presence of a mitochondrial peroxidase. Utilizing a 3,3'-diaminobenzidine (DAB) medium at pH 9.7, the reaction product is localized in the intracristal space, and between the inner and outer membranes of the mitochondria. No inhibitory effects are exerted on the peroxidase reaction by cyanide, azide, or aminotriazole. In addition, the mitochondria appear to have an enzyme which is cytochemically similar to vertebrate cytochrome c-oxidase. The possible physiological significance of the peroxidase is discussed.
D000818:Animals; D002589:Cestoda / Q000201:enzymology*; D003574:Cytochrome c Group / Q000378:metabolism; D006651:Histocytochemistry; D006926:Hymenolepis / Q000201:enzymology* / Q000648:ultrastructure; D008928:Mitochondria / Q000201:enzymology*; D008930:Mitochondria, Liver / Q000201:enzymology; D010544:Peroxidases / Q000378:metabolism*; D051381:Rats
D003574:Cytochrome c Group; D010544:Peroxidases