Isolierung und Aufreinigung des Enzyms Glucose-6-phosphat Dehydrogenase aus Saccharomyces cerevisiae mit der Expanded Bed Adsorption

The ion-exchange chromatography is a popular method for the purification of proteins out of complex solutions. Ion-exchange adsorbents have the advantage of a high chemical stability and are additionally low-priced in comparison with the affinity adsorbents. In this work fundamental statements are made for the purification of glucose-6-phosphat dehydrogenase (G6PDH) out of saccharomyces cerevisiae concerning the application in the enzymatic quantitative measurement of glucose. The G6PDH is fixed at the anion-exchanger: Streamline "t"r"a"d"e"m"a"r"k DEAE and used for a concentration determination of glucose. During the expanded bed adsorption, clarification, concentration and fractionation occurs in one step, presenting a promising development in comparison with the classic multistep reconditioning process. (orig.)Available from TIB Hannover: RA 3251(99/E/18) / FIZ - Fachinformationszzentrum Karlsruhe / TIB - Technische InformationsbibliothekSIGLEDEGerman