Purified tyrosinase T1 was incubated with neuraminidase. The catalytic activity of tyrosinase was essentially retained, after this treatment. The tyrosinase band (Dopa stained) was transformed into a new less anodic form, similar to tyrosinase T2, on disc electrophoresis. The band of protein was also converted to the same position as the Dopa stained. The other hand, the only one PAS stained band of native tyrosinase T1 was splitted into the three slower-moving bands. One was consistent with Dopa and protein stained bands. The other two were much more slower than the former band and completely free of peptide and enzymic activity. The PAS-densitometric value of native tyrosinase T1 was almost equal to those of three separated bands in total. These results suggest that mammalian tyrosinase is a kind of glycoprotein.