Isoenzymic patterns of tyrosinase in the rabbit choroid and retina/retinal pigment epithelium

Tyrosinase in crude extracts from the adult rabbit choroid and retina/retinal pigment epithelium was found to be differently affected by the inhibitors sodium metabisulfite, cyanide, diethyldithiocarbamate and 2,2′-dipyridyl: the latter inhibited the activity in the retina/retinal pigment epithelium extract after 24 hr of incubation, but not that in the choroid. The first three inhibitors, on the other hand, inhibited the activity in the choroid extract, but not in the retina/retinal pigment epithelium extract, after 3 hr of incubation. Both extracts contained one insoluble and two soluble isoenzymes. The mobilities and the apparent molecular weights of the soluble isoenzymes (more markedly so for the most rapidly migrating) differed, as revealed by polyacrylamide gel electrophoresis, resulting in distinct isoenzymic patterns. We suggest that such patterns may be related to the characteristic melanogenic features of the retina/retinal pigment epithelium and choroid.