Rat liver alcohol dehydrogenase. Characterisation of alkylated cysteine residues in the carboxymethylated protein
Rat liver alcohol dehydrogenase. Characterisation of alkylated cysteine residues in the carboxymethylated protein
复制标题
大鼠肝脏乙醇脱氢酶。
DOI：
10.1016/0014-5793(72)80670-7
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发表时间：
1972
期刊：
影响因子：
3.5
通讯作者：
H. Jörnvall
中科院分区：
文献类型：
--
作者：
H. Jörnvall
来自大鼠肝脏的乙醇脱氢酶 (EC 1.1. 1.1) 可以多种形式获得，并且电泳图谱受预处理（例如硫醇）的影响 [1]。对多种形式的解释尚不清楚，但硫醇的作用可能至少在其中一些情况下表明半胱氨酸残基的作用。这些尚未在酶中得到充分表征，但已知大鼠和马蛋白质之间存在一个半胱氨酸差异 [2]。因此，大鼠肝脏乙醇脱氢酶中半胱氨酸（或半胱氨酸）残基数量的测定在该酶的结构研究中具有特别的意义，并且在本工作中进行了报道。在还原和[14C1羧甲基化蛋白的多肽链中发现了16个独特的羧甲基半胱氨酸(CM-半胱氨酸)残基，并给出了它们周围的氨基酸序列。
Alcohol dehydrogenase (EC 1.1. 1.1) from rat liver may be obtained in multiple forms and the electrophoretie pattern is influenced by the pretreatment, eg by thiols [l]. The explanation of the multiple forms is unknown but the effect of thiols may at least in some of these cases suggest a role of cysteine residues. These have not been fully characterized in the enzyme but one cysteine difference is known between the rat and horse proteins [2]. The determination of the number of cysteine (or half-cystine) residues in rat liver alcohol dehydrogenase is therefore of special interest in the structural study of the enzyme and is reported in the present work. 16 Unique carboxymethylcysteine(CM-cysteine) residues were found in the polypeptide chain of the reduced and [14C1 carboxymethylated protein and the amino acid sequences around them are given.