1997 Volume 30 Issue 1 Pages 113-115
The enzymatic histochemical localization of aldehyde oxidase in the rat liver lobule was investigated by use of a tissue protectant, polyvinyl alcohol, with tetra-nitro BT as the final electron acceptor. This method demonstrated the presence of aldehyde oxidase activity in the cytoplasm of liver cells. Distribution of aldehyde oxidase activity in the liver was uneven, being seen mainly in the pericentral rather than the periportal area as with xanthine oxidase. The reaction was not inhibited by TEI-6720 but was markedly inhibited by benzamidine. Results were consistent with those of immunohistochemical localization studies of this enzyme.
