Ultrastructural localization of alpha-OH acid oxidase in peroxisomes with the CeCl3 technique.
alpha-OH acid oxidase activity was demonstrated in peroxisomes of glutaraldehyde-fixed tissues using the CeCl3 cytochemical method. For kidney, alpha-OH butyrate or alpha-OH valerate were used as substrates. These substrates gave much less reaction product in liver peroxisomes. Liver peroxisomes were more reactive with glycolate as substrate. Glycolate gave little or no reaction product in kidney peroxisomes. alpha-keto-glutarate inhibited activity of the enzyme with alpha-OH butyrate as substrate.
D000429:Alcohol Oxidoreductases / Q000032:analysis*; D000818:Animals; D002563:Cerium; D006651:Histocytochemistry; D007202:Indicators and Reagents; D007668:Kidney / Q000201:enzymology / Q000648:ultrastructure; D008099:Liver / Q000201:enzymology / Q000648:ultrastructure; D008297:Male; D008830:Microbodies / Q000201:enzymology* / Q000648:ultrastructure; D008854:Microscopy, Electron; D009940:Organoids / Q000201:enzymology*; D051381:Rats
D007202:Indicators and Reagents; D002563:Cerium; D000429:Alcohol Oxidoreductases; C021380:L-2-hydroxyacid oxidase; C026690:cerous chloride