Yoshimura S, Komatsu N, Watanabe K
Biochim Biophys Acta. 1980 Jan 24;621(1):130-7. doi: 10.1016/0005-2795(80)90068-9.
Glutathione peroxidase was purified from the rat liver to give a single protein band in polyacrylamide gel electrophoresis. Rabbits were immunized with this purified enzyme, and a highly specific anti-glutathione peroxidase antiserum was obtained. Using this antibody, an immunohistochemical technique (the indirect method of peroxidase-labeled antibody) was applied to study the localization of the enzyme in the liver cells. On immunohistochemical observation, glutathione peroxidase was localized exclusively in the cytoplasm of hepatocytes, and a stronger 'immuno-staining' was exhibited in the peripheries of the hepatic lobules than in the central zone.