Characteristics of tyrosinase in B16 melanoma.
Tyrosine hydroxylase, dopa oxidase, and peroxidase activities were studied in soluble fractions of B16 melanoma tumor homogenates by polyacrylamide gel disc electrophoresis. Stained gels were scanned photometrically and gel slices were assayed radiometrically. In these preparations, the two bands of tyrosine hydroxylating activity were completely separated from the peroxidase activity but coincided with two major bands of dopa oxidase activity. The third dopa oxidase band coincided with the single band of peroxidase activity. The soluble fraction of cultured cell homogenates had no peroxidase activity, but the two tyrosine hydroxylase bands coincided exactly with the two dopa oxidase bands. Therefore, in the soluble fraction of the murine melanoma bifunctional tyrosinase does exist as two electrophoretically separable forms which are independent of peroxidase.
D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D008297:Male; D008545:Melanoma / Q000201:enzymology*; D051379:Mice; D008810:Mice, Inbred C57BL; D014442:Monophenol Monooxygenase / Q000378:metabolism; D009374:Neoplasms, Experimental; D010544:Peroxidases / Q000378:metabolism; D010783:Photometry; D012878:Skin Neoplasms / Q000201:enzymology*; D014443:Tyrosine / Q000378:metabolism*; D014446:Tyrosine 3-Monooxygenase / Q000378:metabolism
D014443:Tyrosine; D010544:Peroxidases; D014446:Tyrosine 3-Monooxygenase; D014442:Monophenol Monooxygenase