Inability of murine melanoma melanosomal "tyrosinase" (L-dopa oxidase) to oxidize tyrosine to melanin in polyacrylamide gel systems.
Melanosomal "tyrosinase" (L-dopa) was isolated from trypsin digest of B-16 mouse melanoma melanosomes, using polyacrylamide gel disc electrophoresis. The enzyme was represented by a single band, having characteristics similar to the T1 dopa-positive band observed when using supernatants of crude melanoma homogenates as the source. When gels with this band were incubated in solutions containing tyrosine and dopa in varying ratios , there was no enhancement of melanin formation by tyrosine when compared with incubations in corresponding concentrations of dopa alone. These data further support previous studies in our laboratory demonstrating an inability of so-called mamalian "tyrosinase" to convert tyrosine to melanin; since this enzyme readily converts L-dopa to melanin, it seems more reasonable to term this enzyme an L-dopa oxidase.
D000818:Animals; D004156:Catechol Oxidase / Q000302:isolation & purification / Q000378:metabolism*; D002460:Cell Line; D004591:Electrophoresis, Polyacrylamide Gel; D008543:Melanins / Q000096:biosynthesis*; D008544:Melanocytes / Q000201:enzymology* / Q000648:ultrastructure; D008545:Melanoma / Q000201:enzymology*; D051379:Mice; D008810:Mice, Inbred C57BL; D009374:Neoplasms, Experimental / Q000201:enzymology; D009940:Organoids / Q000201:enzymology* / Q000648:ultrastructure; D010084:Oxidation-Reduction; D014443:Tyrosine / Q000378:metabolism*
D008543:Melanins; D014443:Tyrosine; D004156:Catechol Oxidase