• 文献检索
  • 文档翻译
  • 深度研究
  • 学术资讯
  • Suppr Zotero 插件Zotero 插件
  • 邀请有礼
  • 套餐&价格
  • 历史记录
应用&插件
Suppr Zotero 插件Zotero 插件浏览器插件Mac 客户端Windows 客户端微信小程序
定价
高级版会员购买积分包购买API积分包
服务
文献检索文档翻译深度研究API 文档MCP 服务
关于我们
关于 Suppr公司介绍联系我们用户协议隐私条款
关注我们

Suppr 超能文献

核心技术专利:CN118964589B侵权必究
粤ICP备2023148730 号-1Suppr @ 2026

文献检索

告别复杂PubMed语法,用中文像聊天一样搜索,搜遍4000万医学文献。AI智能推荐,让科研检索更轻松。

立即免费搜索

文件翻译

保留排版,准确专业,支持PDF/Word/PPT等文件格式,支持 12+语言互译。

免费翻译文档

深度研究

AI帮你快速写综述,25分钟生成高质量综述,智能提取关键信息,辅助科研写作。

立即免费体验

Ouabain-binding vesicles from skeletal muscle.

作者信息

Caswell A H, Lau Y H, Brunschwig J P

出版信息

Arch Biochem Biophys. 1976 Oct;176(2):417-30. doi: 10.1016/0003-9861(76)90184-3.

DOI:10.1016/0003-9861(76)90184-3
PMID:136228
Abstract
摘要

相似文献

1
Ouabain-binding vesicles from skeletal muscle.来自骨骼肌的哇巴因结合囊泡。
Arch Biochem Biophys. 1976 Oct;176(2):417-30. doi: 10.1016/0003-9861(76)90184-3.
2
Ouabain-receptor interactions in (Na+ + K+)-ATPase preparations. A contribution to the problem of nonlinear Scatchard plots.
Biochim Biophys Acta. 1976 Dec 2;455(2):287-96. doi: 10.1016/0005-2736(76)90305-9.
3
Isolation of transverse tubules by fractionation of triad junctions of skeletal muscle.通过骨骼肌三联体连接的分级分离来分离横小管
J Biol Chem. 1977 Aug 10;252(15):5565-74.
4
Sodium-potassium stimulated adenosinetriphosphatase of vascular smooth muscle.血管平滑肌钠钾激活的三磷酸腺苷酶
Can J Biochem. 1971 Mar;49(3):376-84. doi: 10.1139/o71-055.
5
Effects of sodium and potassium on binding of ouabain to the transport adenosine triphosphatase.钠和钾对哇巴因与转运三磷酸腺苷酶结合的影响。
J Biol Chem. 1974 Aug 25;249(16):5135-40.
6
Saxitoxin and ouabain binding activity of isolated skeletal muscle membrane as indicators of surface origin and purity.分离的骨骼肌膜的石房蛤毒素和哇巴因结合活性作为表面来源和纯度的指标。
Biochim Biophys Acta. 1983 Jul 27;732(2):412-20. doi: 10.1016/0005-2736(83)90058-5.
7
Preparation and properties of the (Na+ + K+)-ATPase of plasma membranes from Ehrlich ascites cells.艾氏腹水癌细胞质膜(Na⁺ + K⁺)-ATP酶的制备及其性质
Biochim Biophys Acta. 1973 Sep 27;323(1):69-86. doi: 10.1016/0005-2736(73)90432-x.
8
Thermodynamics of the rate of binding of oubain to the sodium, potassium-adenosine triphosphatase.
J Biol Chem. 1974 Aug 25;249(16):5141-7.
9
[3H]-ouabain binding to denervated and innervated skeletal muscle.[3H]-哇巴因与去神经和有神经支配的骨骼肌的结合。
Eur J Pharmacol. 1977 Jun 1;43(3):273-6. doi: 10.1016/0014-2999(77)90027-9.
10
Ouabain binding to the sodium pump.哇巴因与钠泵的结合。
Nature. 1973 Mar 2;242(5392):62-3. doi: 10.1038/242062a0.

引用本文的文献

1
Enrichment of triadic and terminal cisternae vesicles from rabbit skeletal muscle.
J Membr Biol. 2003 Sep 1;195(1):9-20. doi: 10.1007/s00232-003-2037-5.
2
Electron tomography of frozen-hydrated isolated triad junctions.冷冻水合分离三联体连接的电子断层扫描
Biophys J. 2002 Nov;83(5):2491-501. doi: 10.1016/S0006-3495(02)75260-0.
3
Extraction of junctional complexes from triad junctions of rabbit skeletal muscle.从兔骨骼肌三联体连接处提取连接复合体。
J Muscle Res Cell Motil. 1994 Oct;15(5):493-504. doi: 10.1007/BF00121156.
4
Endogenous, Ca(2+)-dependent cysteine-protease cleaves specifically the ryanodine receptor/Ca2+ release channel in skeletal muscle.
J Membr Biol. 1994 Dec;142(3):281-8. doi: 10.1007/BF00233435.
5
Detection and localization of triadin in rat ventricular muscle.大鼠心室肌中三磷酸肌醇受体结合蛋白的检测与定位
J Membr Biol. 1993 Feb;131(3):219-28. doi: 10.1007/BF02260110.
6
Identification of a constituent of the junctional feet linking terminal cisternae to transverse tubules in skeletal muscle.骨骼肌中连接终池与横小管的连接足成分的鉴定。
J Cell Biol. 1982 Jun;93(3):543-50. doi: 10.1083/jcb.93.3.543.
7
Identification and extraction of proteins that compose the triad junction of skeletal muscle.骨骼肌三联体连接复合体组成蛋白的鉴定与提取。
J Cell Biol. 1984 Sep;99(3):929-39. doi: 10.1083/jcb.99.3.929.
8
Monovalent ion and calcium ion fluxes in sarcoplasmic reticulum.肌浆网中的单价离子和钙离子通量
Mol Cell Biochem. 1983;55(1):65-82. doi: 10.1007/BF00229243.
9
Purification of morphologically intact triad structures from skeletal muscle.从骨骼肌中纯化形态完整的三联体结构。
J Cell Biol. 1983 Apr;96(4):1008-16. doi: 10.1083/jcb.96.4.1008.
10
Mechanism of calcium release from skeletal sarcoplasmic reticulum.骨骼肌肌浆网钙释放机制
J Membr Biol. 1982;66(3):193-201. doi: 10.1007/BF01868494.