猴脑乙酰胆碱酯酶的亚基缔合与糖基化

Subunit association and glycosylation of acetylcholinesterase from monkey brain.

作者信息

Liao J, Nørgaard-Pedersen B, Brodbeck U

机构信息

Institute of Biochemistry and Molecular Biology, University of Bern, Switzerland.

出版信息

J Neurochem. 1993 Sep;61(3):1127-34. doi: 10.1111/j.1471-4159.1993.tb03629.x.

DOI:10.1111/j.1471-4159.1993.tb03629.x

PMID:8360678

Abstract

Cercopithecus monkey brain acetylcholinesterase (AChE; EC 3.1.1.7) consists of about 15% hydrophilic, salt-soluble enzyme and 83% amphiphilic, detergent-soluble enzyme. Sucrose density gradient centrifugation showed that hydrophilic, salt-soluble AChE was composed of about 85% tetramer (10.3S) and 15% monomer (3.3S). In amphiphilic, detergent-soluble AChE, 85% tetramer (9.7S), 10% dimer (5.7S), and 5% monomer (3.2S) were seen. The enzyme is N-glycosylated, and no O-linked carbohydrate could be detected. Use of two monoclonal antibodies, one directed against the catalytic subunit and the other against the hydrophobic anchor, gave new insights into the subunit assembly of brain AChE. It is shown that in tetrameric AChE, not all of the subunits are disulfide-bonded and that two populations of tetramers exist, one carrying one and the other carrying two hydrophobic anchors.

摘要

猕猴脑乙酰胆碱酯酶（AChE；EC 3.1.1.7）约15%为亲水性、盐溶性酶，83%为两亲性、去污剂溶性酶。蔗糖密度梯度离心显示，亲水性、盐溶性AChE约85%为四聚体（10.3S），15%为单体（3.3S）。在两亲性、去污剂溶性AChE中，可见85%四聚体（9.7S）、10%二聚体（5.7S）和5%单体（3.2S）。该酶为N-糖基化，未检测到O-连接的碳水化合物。使用两种单克隆抗体，一种针对催化亚基，另一种针对疏水锚定，为脑AChE的亚基组装提供了新的见解。结果表明，在四聚体AChE中，并非所有亚基都通过二硫键连接，且存在两种四聚体群体，一种携带一个疏水锚定，另一种携带两个疏水锚定。