斑纹电鳐电器官中乙酰胆碱受体的轻、重形式：利用重组囊泡进行形态学鉴定 - Suppr

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超能文献

Light and heavy forms of the acetylcholine receptor from Torpedo marmorata electric organ: morphological identification using reconstituted vesicles.

作者信息

Cartaud J, Popot J L, Changeux J P

出版信息

FEBS Lett. 1980 Dec 1;121(2):327-32. doi: 10.1016/0014-5793(80)80374-7.

DOI:10.1016/0014-5793(80)80374-7

PMID:7461135

Abstract

摘要

相似文献

Light and heavy forms of the acetylcholine receptor from Torpedo marmorata electric organ: morphological identification using reconstituted vesicles.斑纹电鳐电器官中乙酰胆碱受体的轻、重形式：利用重组囊泡进行形态学鉴定

FEBS Lett. 1980 Dec 1;121(2):327-32. doi: 10.1016/0014-5793(80)80374-7.

Purification and characterization of the cholinergic receptor protein in its membrane-bound and detergent-soluble forms from the electric organ of Torpedo marmorata.

Biochem Soc Trans. 1977;5(2):511-4. doi: 10.1042/bst0050511.

Translational diffusion coefficient and molecular weight of the acetylcholine receptor from Torpedo marmorata.斑纹电鳐乙酰胆碱受体的平移扩散系数和分子量

FEBS Lett. 1980 May 5;113(2):312-4. doi: 10.1016/0014-5793(80)80616-8.

Identification of the acetylcholine receptor subunit in the lipid bilayer of Torpedo electric organ excitable membranes.电鳐电器官可兴奋膜脂质双分子层中乙酰胆碱受体亚基的鉴定。

J Biol Chem. 1980 Feb 10;255(3):1204-9.

Affinity labelling by bromoacetylcholine of a characteristic subunit in the acetylcholine receptor from muscle and Torpedo electric organ.用溴乙酰胆碱对来自肌肉和电鳐电器官的乙酰胆碱受体中的一个特征亚基进行亲和标记。

FEBS Lett. 1979 Dec 1;108(1):20-4. doi: 10.1016/0014-5793(79)81169-2.

Large-scale purification of the acetylcholine-receptor protein in its membrane-bound and detergent-extracted forms from Torpedo marmorata electric organ.从电鳐电器官中大规模纯化膜结合形式和去污剂提取形式的乙酰胆碱受体蛋白。

Eur J Biochem. 1977 Oct 17;80(1):215-24. doi: 10.1111/j.1432-1033.1977.tb11874.x.

[Purification of a protein binding quinacrine and histrionicotoxin from membrane fragments rich in cholinergic receptors in Torpedo marmorata].[从电鳐富含胆碱能受体的膜片段中纯化结合喹吖因和组氨酰毒的蛋白质]

C R Acad Hebd Seances Acad Sci D. 1977 Nov 21;285(14):1255-8.

Acetylcholine receptors from electroplax membranes: in vitro and in situ properties.

Adv Exp Med Biol. 1982;148:209-22. doi: 10.1007/978-1-4615-9281-5_17.

Reconstitution of a functional acetylcholine receptor. Polypeptide chains, ultrastructure, and binding sites for acetylcholine and local anesthetics.功能性乙酰胆碱受体的重组。多肽链、超微结构以及乙酰胆碱和局部麻醉药的结合位点。

Eur J Biochem. 1980 Sep;110(1):13-33. doi: 10.1111/j.1432-1033.1980.tb04838.x.

Lactoperoxidase catalyzed membrane surface labeling of the acetylcholine receptor from Torpedo californica.乳过氧化物酶催化的加州电鳐乙酰胆碱受体的膜表面标记

Biochem Biophys Res Commun. 1977 Sep 9;78(1):16-22. doi: 10.1016/0006-291x(77)91215-3.

引用本文的文献

Progress in nicotinic receptor structural biology.烟碱型乙酰胆碱受体结构生物学研究进展。

Neuropharmacology. 2020 Jul;171:108086. doi: 10.1016/j.neuropharm.2020.108086. Epub 2020 Apr 7.

Consequences of alkaline treatment for the ultrastructure of the acetylcholine-receptor-rich membranes from Torpedo marmorata electric organ.碱性处理对电鳐电器官富含乙酰胆碱受体的膜超微结构的影响。

J Cell Biol. 1981 Aug;90(2):418-26. doi: 10.1083/jcb.90.2.418.

Electron microscopy of complexes of isolated acetylcholine receptor, biotinyl-toxin, and avidin.分离出的乙酰胆碱受体、生物素化毒素和抗生物素蛋白复合物的电子显微镜检查。

Proc Natl Acad Sci U S A. 1982 Jan;79(2):310-4. doi: 10.1073/pnas.79.2.310.

Physiochemical and immunological properties of acetylcholine receptors from human muscle.来自人体肌肉的乙酰胆碱受体的物理化学和免疫学特性。

Mol Cell Biochem. 1984 Sep;64(1):69-79. doi: 10.1007/BF00420930.

Oligomeric forms of the membrane-bound acetylcholine receptor disclosed upon extraction of the Mr 43,000 nonreceptor peptide.在提取43,000道尔顿的非受体肽后，膜结合型乙酰胆碱受体的寡聚体形式得以展现。

J Cell Biol. 1982 Jan;92(1):60-8. doi: 10.1083/jcb.92.1.60.

Different channel properties of Torpedo acetylcholine receptor monomers and dimers reconstituted in planar membranes.在平面膜中重组的电鳐乙酰胆碱受体单体和二聚体的不同通道特性。

Proc Natl Acad Sci U S A. 1984 Oct;81(19):6222-6. doi: 10.1073/pnas.81.19.6222.

Transmembrane topography of the nicotinic acetylcholine receptor delta subunit.烟碱型乙酰胆碱受体δ亚基的跨膜拓扑结构

EMBO J. 1987 Dec 1;6(12):3619-26. doi: 10.1002/j.1460-2075.1987.tb02693.x.

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