The reciprocal relationship between melanization and tyrosinase activity in melanosomes (melanin granules).
The reciprocal relationship between melanization and tyrosinase activity in melanosomes (melanin granules).
复制标题
黑色素体(黑色素颗粒)中黑色化与酪氨酸酶活性之间的相互关系。
DOI:
10.1093/oxfordjournals.jbchem.a127360
复制
发表时间:
1961
影响因子:
2.7
通讯作者:
Thomas B. Fitzpatrick
中科院分区:
文献类型:
--
作者:
M. Seiji;Thomas B. Fitzpatrick
In mammals, melanin pigment is synthe sized in a speciffc cell, the melanocyte, by the action of a copper-containing oxidase, tyrosinase (1•`3). This enzyme catalyzes the aerobic oxidation of tyrosine, the precursor of melanin, to a monomer, 5,6-dihydroxy indole; this monomer, in turn, is transformed into a large polymer which is probably at tached through its quinone linkages to the amino or sulfhydryl groups of the protein matrix of the pigment granule. It has been shown that mammalian tyrosinase is attached to a specific cytoplasmic particle (4, 5). The name " melanosome " has been proposed for these distinctive, enzymatically active particles which are the site of melanin formation and are found only within the cytoplasm of the melanocyte (6). Melanosomes have been shown by biochemical and electronmicroscopic studies to be different from mitochondia (6). Electronmicroscopy has revealed the mor