High resolution gel chromatography of proteins

Autor: Burkhardt Dahlmann, Lothar Kuehn, Malte Rutschmann, Hans Reinauer
Rok vydání: 1982
Předmět:
Zdroj: Analytical biochemistry. 124(1)
ISSN: 0003-2697
Popis: The protein fractionation pattern on three different gels—Sephadex G-75 superfine, Ultrogel AcA 54, and Bio-Gel P-100 minus 400 mesh—has been compared. Analysis of the column eluates by sodium dodecyl sulfate-polyacrylamide gel electrophoresis demonstrated Bio-Gel P-100 to be a gel with very high separation efficiency, allowing complete resolution of proteins differing in M r by as little as 5000. The method is simple and inexpensive and allows the investigator to perform protein fractionations with resolution similar to that possible by high-performance liquid chromatography, but at a preparative scale and with little risk of protein denaturation.
Databáze: OpenAIRE