Identification of covalently attached fatty acids in the hydrophobic membrane-binding domain of human erythrocyte acetylcholinesterase.
Identification of covalently attached fatty acids in the hydrophobic membrane-binding domain of human erythrocyte acetylcholinesterase.
复制标题
人红细胞乙酰胆碱酯酶疏水膜结合域中共价连接的脂肪酸的鉴定。
DOI：
10.1016/0006-291x(85)90950-7
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发表时间：
1985
影响因子：
3.1
通讯作者：
Rosenberry,TL
中科院分区：
文献类型：
--
作者：
Roberts,WL;Rosenberry,TL
人红细胞乙酰胆碱酯酶是一种两亲性酶，其疏水膜结合域可以选择性地用亲脂性光试剂标记，并通过木瓜蛋白酶消化去除。在本文中，我们表明，甲醇分解释放共价结合的脂肪酸从疏水结构域，从而确认该结构域是一个共价连接的糖脂在酶亚基C-末端。每摩尔结构域释放约1摩尔饱和脂肪酸和1摩尔不饱和脂肪酸。由于主要的不饱和脂肪酸（22：4和22：5）是人红细胞膜中酯化脂肪酸池的次要组分，因此糖脂的组装必须涉及选定的不饱和脂肪酸池。
Human erythrocyte acetylcholinesterase is an amphipathic enzyme whose hydrophobic membrane-binding domain can be selectively labeled with a lipophilic photoreagent and removed by digestion with papain. In this paper we demonstrate that methanolysis releases covalently bound fatty acids from the hydrophobic domain and thus confirm that this domain is a covalently linked glycolipid at the enzyme subunit C-terminus. About one mole of saturated and one mole of unsaturated fatty acids were released per mole of domain. Since the predominant unsaturated fatty acids (22:4 and 22:5) are minor components of the esterified fatty acid pool in human erythrocyte membranes, assembly of the glycolipid must involve a selected unsaturated fatty acid pool.