A rapid and simple method for isoelectric focusing of proteins separated by SDS-polyacrylamide gel electrophoresis was described. The focusing system was composed of a polyacrylamide gel layer (7 cm in height) and a solution layer (1.2 cm in height) superimposed on the gel layer. Both layers contain
Quantitative analysis of proteins by the use of SDS-polyacrylamide-gel electrophoresis
โ Scribed by Tezro Asao
- Publisher
- Elsevier Science
- Year
- 1977
- Tongue
- English
- Weight
- 547 KB
- Volume
- 77
- Category
- Article
- ISSN
- 0003-2697
No coin nor oath required. For personal study only.
โฆ Synopsis
Insulin, hemoglobin, egg albumin, gamma globulin, bovine serum albumin, and phosphorylase a were separated by SDS-polyacrylamide gel electrophoresis, and continuously recovered for quantitation in aqueous solution using a new technique. The proteins, which were eluted in the order of their molecular weight, were determined by their absorbance at 200 nm. The recovery of the eluted protein fractions was virtually complete.
๐ SIMILAR VOLUMES
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