Leishmania donovani: ultrastructural localization of diaminobenzidine reactivity in the amastigotes.
Intracellular amastigotes of Leishmania donovani obtained from spleens of infected hamsters were studied by means of the diaminobenzidine technique for the presence of cytochromes and the activities of cytochrome oxidase and peroxidase. In the absence of H2O2, the oxidation of DAB, evidenced by electron-dense deposits localized on the cristae, inclusions, and enveloping membranes of the mitochondria and kinetoplast, revealed the activity of the cytochrome oxidase and the presence of the cytochromes. The increased deposition of DAB oxidation especially on the enveloping membranes in the presence of H2O2 suggests the activity of a peroxidase, probably cytochrome c peroxidase.
D015100:3,3'-Diaminobenzidine; D000818:Animals; D001560:Benzidines; D006224:Cricetinae; D003578:Cytochrome-c Peroxidase / Q000378:metabolism; D003580:Cytochromes / Q000302:isolation & purification*; D003576:Electron Transport Complex IV / Q000378:metabolism; D006651:Histocytochemistry; D002479:Inclusion Bodies / Q000201:enzymology; D007891:Leishmania / Q000201:enzymology / Q000648:ultrastructure*; D007898:Leishmaniasis, Visceral / Q000469:parasitology*; D008928:Mitochondria / Q000201:enzymology; D009940:Organoids / Q000201:enzymology; D013154:Spleen / Q000469:parasitology
D001560:Benzidines; D003580:Cytochromes; D015100:3,3'-Diaminobenzidine; D003578:Cytochrome-c Peroxidase; D003576:Electron Transport Complex IV