Metallothionein as a trap for reactive organic intermediates.
Metallothionein as a trap for reactive organic intermediates.
复制标题
金属硫蛋白作为反应性有机中间体的陷阱。
DOI：
10.1007/978-1-4757-0674-1_46
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发表时间：
1981
影响因子：
--
通讯作者：
Cagen,SZ
中科院分区：
文献类型：
--
作者：
Klaassen,CD;Cagen,SZ
金属硫蛋白是一种镉结合蛋白，最早由Margoshes和Vallee（1957）从马肾皮质中分离出来。它是一种低分子量（约6000）的蛋白质，具有非常高的半胱氨酸含量（约30%的氨基酸残基），不含芳香氨基酸和组氨酸（Kagi et al., 1974）。类似的蛋白质已经从人类的肝脏和/或肾脏（Pulido et al., 1966; Buhler and Kagi, 1974）和许多其他物种中分离出来。测定了马肾金属硫蛋白（Kojima etal ., 1976）和小鼠肝金属硫蛋白（Huange etal ., 1977）的氨基酸序列。这两个来源的金属硫蛋白都含有20个半胱氨酸残基（总共61个氨基酸残基），在氨基酸序列上具有显著的结构同源性。
Metallothionein is a cadmium-binding protein first isolated from equine renal cortex by Margoshes and Vallee (1957). It is a protein of low molecular weight (about 6,000) having a very high cysteine content (about 30% of the amino acid residues) and an absence of aromatic amino acids and histidine (Kagi et al., 1974). Similar proteins have been isolated from the liver and/or kidney of humans (Pulido et al., 1966; Buhler and Kagi, 1974), and many other species. The amino acid sequences of equine renal metallothionein (Kojima et al., 1976) and hepatic metallothionein from mice (Huange et al., 1977) have been determined. The metallothionein from these two sources both contain 20 cysteine residues (out of a total of 61 amino acid residues) and remarkable structural homology in the amino acid sequence.