Tyrosinase as glycoprotein

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 als...

Full description

Saved in:
Bibliographic Details
Published in:Archiv für dermatologische Forschung 1975-01, Vol.252 (3), p.211-216
Main Authors: Miyazaki, K, Otaki, N
Format: Article
Language:English
Subjects:
Animals
Catechol Oxidase
Chemical Phenomena
Chemistry
Densitometry
Electrophoresis, Polyacrylamide Gel
Glycoproteins
Hydrolysis
In Vitro Techniques
Isoelectric Point
Isoenzymes - metabolism
Melanoma - enzymology
Mice
Neoplasms, Experimental
Neuraminidase
Sialic Acids - analysis
Skin Neoplasms - enzymology
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:0003-9187
0340-3696
1432-069X
DOI:10.1007/BF00557921