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Molecular weight estimation of Triton X-100 solubilized proteins by polyacrylamide gel electrophoresis.

作者信息

Hearing V J, Klingler W G, Ekel T M, Montague P M

出版信息

Anal Biochem. 1976 May 7;72:113-22. doi: 10.1016/0003-2697(76)90512-1.

DOI:10.1016/0003-2697(76)90512-1
PMID:942041
Abstract
摘要

相似文献

1
Molecular weight estimation of Triton X-100 solubilized proteins by polyacrylamide gel electrophoresis.
Anal Biochem. 1976 May 7;72:113-22. doi: 10.1016/0003-2697(76)90512-1.
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Purification and analysis of mitochondrial membrane proteins on nondenaturing gradient polyacrylamide gels.
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Determination of Triton X-100 binding to membrane proteins by polyacrylamide gel electrophoresis.通过聚丙烯酰胺凝胶电泳法测定Triton X-100与膜蛋白的结合情况。
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Effects of triton X-100 on gel electrophoresis and gel chromatography of histones. Possible binding to helical regions.曲拉通X-100对组蛋白凝胶电泳和凝胶色谱的影响。与螺旋区域的可能结合。
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Resolution of hemoglobin subunits by electrophoresis in acid urea polyacrylamide gels containing Triton X-100.在含有Triton X - 100的酸性尿素聚丙烯酰胺凝胶中通过电泳分离血红蛋白亚基。
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Concanavalin A-reactive protein of rabbit thymocyte plasma membranes: analysis by crossed immune electrophoresis and sodium dodecylsulfate/polyacrylamide gel electrophoresis.兔胸腺细胞质膜的伴刀豆球蛋白A反应性蛋白:通过交叉免疫电泳和十二烷基硫酸钠/聚丙烯酰胺凝胶电泳进行分析
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Western blotting and immunochemical detection of histones electrophoretically resolved on acid-urea-triton- and sodium dodecyl sulfate-polyacrylamide gels.在酸性尿素- Triton和十二烷基硫酸钠-聚丙烯酰胺凝胶上电泳分离的组蛋白的蛋白质免疫印迹法和免疫化学检测。
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Hemoglobin Hamilton or alpha 2 beta 2 11(A8)Val leads to Ile: a silent beta-chain variant detected by Triton X-100 acid-urea polyacrylamide gel electrophoresis.
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Fluorescent properties of histone-1-anilinonaphthalene 8-sulfonate complexes in the presence of denaturant agents: application to the rapid staining of histones in urea and Triton-urea-polyacrylamide gels.
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Separation of histone variants and post-translationally modified isoforms by triton/acetic acid/urea polyacrylamide gel electrophoresis.通过Triton/乙酸/尿素聚丙烯酰胺凝胶电泳分离组蛋白变体和翻译后修饰的异构体。
Curr Protoc Mol Biol. 2001 May;Chapter 21:Unit 21.2. doi: 10.1002/0471142727.mb2102s45.

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