Electrophoretic elution of proteins from polyacrylamide gel slices
✍ Scribed by Peter Strålfors; Per Belfrage
- Publisher
- Elsevier Science
- Year
- 1983
- Tongue
- English
- Weight
- 452 KB
- Volume
- 128
- Category
- Article
- ISSN
- 0003-2697
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✦ Synopsis
A method for electrophoretic elution of proteins from polyacrylamide gel slices is described. Eluted proteins were retained by a discontinuous conductivity gradient (M. Otto and M. Snejdárková, Anal. Biochem. 111, 111-114 (1981)). The method has been adapted to slices from slab gels and gels that have been stained and destained. Proteins were eluted as their sodium dodecyl sulfate complexes. Minute amounts of proteins (0.1 microgram) were recovered in high yield (85-95%) in 2 h in less than 0.1 ml volume.
📜 SIMILAR VOLUMES
A method for recovery of polypeptidcs from polyacrylamide gels by electrophoretic elution in a commercially available concentrator, the Amicon-Centricon sample reservoir, has been devised. The recoveries were greater than 90% with four different polypeptides tested ( 12.5 to 80 kDa). After elution,
It is shown that the contribution of the gel itself to amino acid compositions of proteins eluted from polyacrylamide gels is significant (especially at low protein-to-gel ratios), linearly related to the volume of the gel slices eluted, and, when applied as a correction to amino acid composition da