Removal of covalently bound inositol from Torpedo acetylcholinesterase and mammalian alkaline phosphatases by deamination with nitrous acid. Evidence for a common membrane-anchoring structure.
Removal of covalently bound inositol from Torpedo acetylcholinesterase and mammalian alkaline phosphatases by deamination with nitrous acid. Evidence for a common membrane-anchoring structure.
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通过用亚硝酸脱氨基，从鱼雷乙酰胆碱酯酶和哺乳动物碱性磷酸酶中去除共价结合的肌醇。
DOI：
10.1042/bj2410615
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发表时间：
1987
期刊：
影响因子：
--
通讯作者：
Silman,I
中科院分区：
文献类型：
--
作者：
Low,MG;Futerman,AH;Ackermann,KE;Sherman,WR;Silman,I
我们早期的证据表明乙酰胆碱酯酶和碱性磷酸酶都通过共价连接的磷脂酰肌醇锚定在细胞表面[Low, Futerman, Ferguson & Silman (1986) Trends Biochem。科学。 11, 212-215]。我们现在提供基于亚硝酸脱氨反应的化学数据，表明在两种蛋白质中，磷脂酰肌醇部分通过糖苷键连接到带有游离氨基的糖残基。
Our earlier evidence suggested that both acetylcholinesterase and alkaline phosphatase are anchored to the cell surface via covalently-attached phosphatidylinositol [Low, Futerman, Ferguson & Silman (1986) Trends Biochem. Sci. 11, 212-215]. We now present chemical data, based upon a nitrous acid deamination reaction, showing that in both proteins the phosphatidylinositol moiety is attached through a glycosidic linkage to a sugar residue bearing a free amino group.