Peptide production from proteins separated by sodium dodecyl-sulfate polyacrylamide gel electrophoresis
β Scribed by Charles E. Prussak; Melissa T. Almazan; Ben Y. Tseng
- Book ID
- 107714785
- Publisher
- Elsevier Science
- Year
- 1989
- Tongue
- English
- Weight
- 638 KB
- Volume
- 178
- Category
- Article
- ISSN
- 0003-2697
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π SIMILAR VOLUMES
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
High-performance capillary sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) has been developed for the separation and molecular weight (MW) determination of peptides and proteins. In this work, acrylamide was polymerized in fused-silica capillaries of 75 microns I.D. and 10 or 20
## Abstract As a followβup of our previous report (__Anal. Chem.__ 2007, __79__, 821β827) on analytical SDSβPAGE focusing, a refinement of the method for separation of peptides in the small to medium __M__~r~ range (0.5β10β kDa) is here reported, based on a shallow gradient of immobilized positive c
Capillary sodium dodecyl sulfate-gel electrophoresis, a one-dimensional version of the well-established planar analytical method of SDS-polyacrylamide gel electrophoresis, has proven a powerful new microanalytical method for the separation of protein molecules according to their size. In this paper