Saturation transfer electron paramagnetic resonance on membrane bound proteins. II-Absence of rotational diffusion of the cholinergic receptor protein in Torpedo marmorata membrane fragments.

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作者信息

Rousselet A, Devaux P F

出版信息

Biochem Biophys Res Commun. 1977 Sep 9;78(1):448-54. doi: 10.1016/0006-291x(77)91275-x.

DOI:10.1016/0006-291x(77)91275-x

PMID:199171

Abstract

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相似文献

Saturation transfer electron paramagnetic resonance on membrane bound proteins. II-Absence of rotational diffusion of the cholinergic receptor protein in Torpedo marmorata membrane fragments.

Biochem Biophys Res Commun. 1977 Sep 9;78(1):448-54. doi: 10.1016/0006-291x(77)91275-x.

[Importance of protein-protein interactions for the structural integrity of membrane framents from Torpedo marmorata electric organ].[蛋白质-蛋白质相互作用对电鳐电器官膜片段结构完整性的重要性]

C R Seances Acad Sci D. 1979 Sep 24;289(5):461-3.

Effects of temperature, lipid modification and pH on the mobility of the major proteins of the receptor-rich membranes from Torpedo marmarata.温度、脂质修饰和pH对电鳐富含受体的膜中主要蛋白质流动性的影响。

Biochim Biophys Acta. 1981 Nov 6;648(2):169-85. doi: 10.1016/0005-2736(81)90032-8.

X-ray diffraction study of membrane fragments rich in acetylcholine receptor protein prepared from the electric organ of Torpedo marmorata.对从多纹电鳐电器官制备的富含乙酰胆碱受体蛋白的膜片段进行的X射线衍射研究。

FEBS Lett. 1974 Mar 15;40(1):130-3. doi: 10.1016/0014-5793(74)80910-5.

The rotational diffusion of the acetylcholine receptor in Torpeda marmorata membrane fragments studied with a spin-labelled alpha-toxin: importance of the 43 000 protein(s).用自旋标记的α-毒素研究电鳐膜片段中乙酰胆碱受体的旋转扩散：43000蛋白的重要性

EMBO J. 1982;1(4):439-45. doi: 10.1002/j.1460-2075.1982.tb01188.x.

Presence of a lattice structure in membrane fragments rich in nicotinic receptor protein from the electric organ of Torpedo marmorata.在来自多纹电鳐电器官的富含烟碱样受体蛋白的膜碎片中存在晶格结构。

FEBS Lett. 1973 Jun 15;33(1):109-13. doi: 10.1016/0014-5793(73)80171-1.

Saturation transfer electron paramagnetic resonance on membrane-bound proteins. I-Rotational diffusion of rhodopsin in the visual receptor membrane.

Biochem Biophys Res Commun. 1977 Sep 9;78(1):442-7. doi: 10.1016/0006-291x(77)91274-8.

Phospholipid chain immobilization and steroid rotational immobilization in acetylcholine receptor-rich membranes from Torpedo marmorata.电鳐富含乙酰胆碱受体的膜中磷脂链固定化和类固醇旋转固定化

Biochim Biophys Acta. 1981 Jul 6;645(1):97-101. doi: 10.1016/0005-2736(81)90516-2.

Fluidity of the lipids next to the acetylcholine receptor protein of torpedo membrane fragments. Use of amphiphilic reversible spin-labels.电鳐膜片段中乙酰胆碱受体蛋白旁脂质的流动性。两亲性可逆自旋标记物的应用。

Biochemistry. 1977 Mar 8;16(5):841-8. doi: 10.1021/bi00624a005.

The amino-terminal sequence of the 40,000 molecular weight subunit of the acetylcholine receptor protein from Torpedo marmorata.

FEBS Lett. 1979 Aug 1;104(1):99-105. doi: 10.1016/0014-5793(79)81092-3.

引用本文的文献

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.

EMBO J. 1982;1(4):439-45. doi: 10.1002/j.1460-2075.1982.tb01188.x.

Spin-label studies of the lipid and protein components of erythrocyte membranes. A comparison of electron paramagnetic resonance and saturation transfer electron paramagnetic resonance methods.红细胞膜脂质和蛋白质成分的自旋标记研究。电子顺磁共振与饱和转移电子顺磁共振方法的比较。

Biophys J. 1981 Feb;33(2):253-62. doi: 10.1016/S0006-3495(81)84886-2.

Quantitative studies on the localization of the cholinergic receptor protein in the normal and denervated electroplaque from Electrophorus electricus.关于电鳗正常及去神经电板中胆碱能受体蛋白定位的定量研究。

J Cell Biol. 1978 Oct;79(1):200-16. doi: 10.1083/jcb.79.1.200.

Large-scale rotational motions of proteins detected by electron paramagnetic resonance and fluorescence.通过电子顺磁共振和荧光检测到的蛋白质大规模旋转运动。

Biophys J. 1978 Nov;24(2):439-62. doi: 10.1016/S0006-3495(78)85394-6.

Immobilized lipid in acetylcholine receptor-rich membranes from Torpedo marmorata.来自电鳐富含乙酰胆碱受体的膜中的固定化脂质。

Proc Natl Acad Sci U S A. 1978 Sep;75(9):4329-33. doi: 10.1073/pnas.75.9.4329.

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