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Conversion of particulate tyrosinase to soluble form and to desialylated tyrosinase in human malignant melanoma
Author(s) -
Nishioka Kenji
Publication year - 1977
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(77)80445-6
Subject(s) - tyrosinase , citation , melanoma , cancer , medicine , chemistry , library science , cancer research , computer science , biochemistry , enzyme
Studies of mammalian tyrosinase (o&phenol: 02 oxidoreductase, EC 1.10.3.1) a key enzyme in melanogenesis, have been conducted principally with soluble forms (T’ faster, T2 slower migrating tyrosinases by gel electrophoresis) obtained from mouse and hamster melanoma [l--S] and these T’ and T2 tyrosinases are considered as isozymes [ 5,6] , However, mammalian melanocytes are known to contain active tyrosinase in both soluble and insoluble melanosome (melanin-producing organelle)bound (T3) forms [2,3] The majority of tyrosinase activity from mouse and human melanoma tissue is in particulate form [3,6,7] . Recently it has been shown by serological studies that human soluble tyrosinase is a glycoprotein [8]. This communication describes the partial purification of tyrosinase with concanavalin A (Con A) affinity chromatography and demonstrates the interconversion of the different enzymes forms (T' , T2, and T3).