Immunohistochemistry of the monkey retina with a monoclonal antibody against subunit V of cytochrome c oxidase.
A monoclonal antibody against subunit V of cytochrome c oxidase was newly prepared from purified bovine heart muscle enzyme. This antibody showed cross-reactivity against the bovine and the human cytochrome c oxidase on Western blot. Cytochrome c oxidase in paraffin embedded sections of monkey retinas and optic nerves was examined immunohistochemically using the monoclonal antibody. The inner segment of cone and rod photoreceptors, the inner nuclear layer and the inner plexiform layer showed marked reactivities. The optic nerve fiber axons also showed high reactivities, with more in the unmyelinated fibers peripheral to the lamina cribrosa. These immunohistochemical results using the antibody are mostly agreeable with previously reported histochemical localization of cytochrome c oxidase activity in the retina, but there were some noticeable differences in the plexiform layers.
Isashiki
Y
Y
Department of Ophthalmology, Kagoshima University Faculty of Medicine, Japan.
Nakagawa
M
M
Higuchi
I
I
D000818:Animals; D000911:Antibodies, Monoclonal; D000918:Antibody Specificity / Q000276:immunology; D015153:Blotting, Western; D002417:Cattle; D002846:Chromatography, Affinity; D003576:Electron Transport Complex IV / Q000302:isolation & purification*; D004591:Electrophoresis, Polyacrylamide Gel; D007124:Immunoenzyme Techniques; D008251:Macaca; D051379:Mice; D008807:Mice, Inbred BALB C; D009900:Optic Nerve / Q000201:enzymology; D012160:Retina / Q000201:enzymology*
D000911:Antibodies, Monoclonal; D003576:Electron Transport Complex IV