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来自兔淋巴细胞和红细胞的糖脂锚定型乙酰胆碱酯酶对磷脂酰肌醇特异性磷脂酶C的敏感性不同。

Glycolipid-anchored acetylcholinesterases from rabbit lymphocytes and erythrocytes differ in their sensitivity to phosphatidylinositol-specific phospholipase C.

作者信息

Richier P, Arpagaus M, Toutant J P

机构信息

Différenciation cellulaire et Croissance, Centre INRA de Montpellier, France.

出版信息

Biochim Biophys Acta. 1992 Nov 23;1112(1):83-8. doi: 10.1016/0005-2736(92)90257-m.

DOI:10.1016/0005-2736(92)90257-m
PMID:1329966
Abstract

The type of membrane association of acetylcholinesterase (AChE, EC 3.1.1.7) was studied in rabbit lymphocytes and erythrocytes. In both cases, the unique AChE molecular form was an amphiphilic dimer (referred to as G2a) anchored in the membrane by a glycosylphosphatidylinositol. In lymphocytes, G2a AChE was directly converted into its hydrophilic G2h counterpart by a treatment with Bacillus thuringiensis phosphatidylinositol-phospholipase C (PI-PLC, EC 3.1.4.10). In erythrocytes, AChE was resistant to PI-PLC but was rendered sensitive by a prior deacylation with alkaline hydroxylamine. This observation suggests that, as previously reported for human erythrocyte AChE, an acylation of the inositol ring in the glycolipid anchor of rabbit erythrocyte AChE (that does not occur in lymphocytes) prevents the cleavage.

摘要

在兔淋巴细胞和红细胞中研究了乙酰胆碱酯酶(AChE,EC 3.1.1.7)的膜结合类型。在这两种情况下,独特的AChE分子形式都是通过糖基磷脂酰肌醇锚定在膜中的两亲性二聚体(称为G2a)。在淋巴细胞中,苏云金芽孢杆菌磷脂酰肌醇 - 磷脂酶C(PI - PLC,EC 3.1.4.10)处理可将G2a AChE直接转化为其亲水性G2h对应物。在红细胞中,AChE对PI - PLC具有抗性,但用碱性羟胺预先脱酰化后则变得敏感。该观察结果表明,如先前关于人红细胞AChE的报道,兔红细胞AChE糖脂锚中肌醇环的酰化(淋巴细胞中不发生)可防止裂解。

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1
Glycolipid-anchored acetylcholinesterases from rabbit lymphocytes and erythrocytes differ in their sensitivity to phosphatidylinositol-specific phospholipase C.来自兔淋巴细胞和红细胞的糖脂锚定型乙酰胆碱酯酶对磷脂酰肌醇特异性磷脂酶C的敏感性不同。
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Amphiphilic, glycophosphatidylinositol-specific phospholipase C (PI-PLC)-insensitive monomers and dimers of acetylcholinesterase.两亲性、糖基磷脂酰肌醇特异性磷脂酶C(PI-PLC)不敏感的乙酰胆碱酯酶单体和二聚体。
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