鲽金属硫蛋白的纯化及特性，一种来自鲽（欧洲比目鱼）肝脏的镉结合蛋白。
Purification and properties of plaice metallothionein, a cadmium-binding protein from the liver of the plaice (Pleuronectes platessa).
作者信息
Overnell J, Coombs T L
出版信息
Biochem J. 1979 Nov 1;183(2):277-83. doi: 10.1042/bj1830277.
Abstract
A low-molecular-weight protein induced in the liver of the plaice (Pleuronectes platessa) by exposure to cadmium was purified and characterized. It is closely similar to mammalian metallothioneins in all of its properties in that it is a single-chain cadmium-binding protein of approx. 7000 mol.wt. with a high cysteine content (31 mol%) and no aromatic amino acid residues. The thiol groups of the cysteine residues complex with the cadmium in a SH/Cd molar ratio of 3:1 and produce a characteristic absorption maximum at 250 nm. Unlike the mammalian metallothioneins, however, metal analyses reveal only traces of zinc and copper in addition to cadmium. The presence of carbohydrate previously assumed from a positive reaction with periodic acid/Schiff reagent has now been disproved, and the positive reaction attributed to interaction with the thiol groups in the protein.
摘要
通过镉暴露在欧鳎（Pleuronectes platessa）肝脏中诱导产生的一种低分子量蛋白质被纯化并进行了特性鉴定。它在所有特性上都与哺乳动物金属硫蛋白非常相似，即它是一种单链镉结合蛋白，分子量约为7000道尔顿，半胱氨酸含量高（31摩尔%）且无芳香族氨基酸残基。半胱氨酸残基的巯基与镉以3:1的SH/Cd摩尔比络合，并在250纳米处产生特征性吸收峰。然而，与哺乳动物金属硫蛋白不同的是，金属分析表明除镉外仅含有痕量的锌和铜。先前通过与高碘酸/席夫试剂的阳性反应推测存在的碳水化合物现在已被证伪，阳性反应归因于与蛋白质中巯基的相互作用。
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