Evidence of the presence of extraperoxisomal catalase in chloragogen cells of the earthworm, Lumbricus terrestris L.
The DAB reactivity of the midintestine of the earthworm, consisting of epithelial layer, muscle layer, and chloragogen tissue, was examined electron microscopically. Besides the mitochondrial membranes of the examined cell types and the hemoglobin content of the blood vessels and chloragogen cells, a considerable DAB reactivity was found in the whole cytosol of the chloragocytes. The DAB reaction of the cytosol was more intensive when incubation medium for catalase, less intensive when incubation medium for peroxidase, was used and did not occur when H2O2 was omitted. Cytosol of the chloragogen cells was isolated and preliminary assay of catalase and peroxidase activities was made. Cytosol samples showed moderate peroxidase activity, but catalase activity measured by the decomposition of hydrogen peroxide showed a very high rate. Catalase and peroxidase activities of the cytosol were heat-sensitive and might have been inhibited by azide and cyanide, respectively. Results prove the assumption that the intensive DAB reactivity of the chloragocyte cytosol is caused by its extraperoxisomal catalase content.
D000818:Animals; D001386:Azides / Q000494:pharmacology; D002374:Catalase / Q000032:analysis* / Q000378:metabolism; D003486:Cyanides / Q000494:pharmacology; D003600:Cytosol / Q000201:enzymology; D006651:Histocytochemistry; D006358:Hot Temperature; D006861:Hydrogen Peroxide / Q000378:metabolism; D007422:Intestines / Q000201:enzymology; D009835:Oligochaeta / Q000201:enzymology*; D010544:Peroxidases / Q000378:metabolism
D001386:Azides; D003486:Cyanides; D006861:Hydrogen Peroxide; D010544:Peroxidases; D002374:Catalase