Efficient method for visualization and isolation of proteins resolved in polyacrylamide gels.

Efficient method for visualization and isolation of proteins resolved in polyacrylamide gels.
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DOI:
10.1016/s0021-9673(01)92699-8
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发表时间:
1984
期刊:
Journal of chromatography
影响因子:
--
通讯作者:
R. T. Francis;J. Davie;M. Sayre;E. Rocha;F. Ziemer;G. Riedel
R. T. Francis;J. Davie;M. Sayre;E. Rocha;F. Ziemer;G. Riedel
中科院分区:
其他
文献类型:
--
作者:
R. T. Francis;J. Davie;M. Sayre;E. Rocha;F. Ziemer;G. Riedel

文献摘要

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Polyacrylamide gel electrophoresis is a popular method used to purify proteins for reconstitution experiments, amino acid composition and sequence determination. In this report we describe methods that will be of general use in the isolation and characterization of proteins and the benefits of substituting boric acid for glycine in the electrophoresis tray buffers. We also described how proteins resolved in a variety of gel systems (including those containing sodium dodecyl sulfate) may be rapidly visuallized with 8-anilino-1-naphthalene sulfonic acid and efficiently transferred to a second gel for two-dimensional gel analysis, or isolated by electroelution for subsequent characterization.