๐”– Bobbio Scriptorium
โœฆ   LIBER   โœฆ

Recovery of Native Proteins from Preparative Electrophoresis Gel Slices by Reverse Polarity ElutioN

โœ Scribed by Abramovitz, Aaron S.; Randolph, Verrell; Mehra, Aruna; Chn'stakos, Sylvia


Book ID
121738803
Publisher
Informa UK (Taylor & Francis)
Year
1984
Tongue
English
Weight
643 KB
Volume
14
Category
Article
ISSN
0032-7484

No coin nor oath required. For personal study only.


๐Ÿ“œ SIMILAR VOLUMES


Preparative elution of proteins from nit
โœ B.S. Parekh; H.B. Mehta; M.D. West; R.C. Montelaro ๐Ÿ“‚ Article ๐Ÿ“… 1985 ๐Ÿ› Elsevier Science ๐ŸŒ English โš– 769 KB

Various conditions were analyzed and optimized for the preparative elution of proteins from nitrocellulose membranes after transfer from sodium dodecyl sulfate (SDS)-polyacrylamide gels. The efficiency of elution was best using pyridine or acetonitrile elution solvents, intermediate for buffer conta

Recovery of SDS-proteins from polyacryla
โœ Barry R. Ziola; Douglas G. Scraba ๐Ÿ“‚ Article ๐Ÿ“… 1976 ๐Ÿ› Elsevier Science ๐ŸŒ English โš– 394 KB

A method is described which permits the purification of proteins in quantities necessary for physicochemical characterization. The protein to be purified is separated from contaminants by electrophoresis in a number of sodium dodecyl sulfate (SDS)-containing polyacrylamide disc gels. The region of e

Preparative isolation of protein complex
โœ Holger Seelert; Frank Krause ๐Ÿ“‚ Article ๐Ÿ“… 2008 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 471 KB

## Abstract Due to its unmatched resolution, gel electrophoresis is an indispensable tool for the analysis of diverse biomolecules. By adaptation of the electrophoretic conditions, even fragile protein complexes as parts of intracellular networks migrate through the gel matrix under sustainment of

Quantitation of proteins by elution of C
โœ Eric H. Ball ๐Ÿ“‚ Article ๐Ÿ“… 1986 ๐Ÿ› Elsevier Science ๐ŸŒ English โš– 424 KB

A simple method for the extraction of Coomassie brilliant blue R from stained protein bands excised from polyacrylamide gels is described. Spectrophotometric measurement of the eluted dye forms the basis of a sensitive assay to quantitate proteins in gels in the range 0.5-10 micrograms. The method r