An enrichment procedure for a highly active T5-receptor preparation by DEAE-cellulose ion-exchange chromatography in Triton X-100 containing solution at elevated temperatures.
This paper describes the purification of a minor outer membrane protein from Escherichia coli B by repeated DEAE-cellulose ion-exchange chromatography at 40 degrees C in phosphate buffer containing 2% Triton X-100. A 480-fold enrichment relative to a crude preparation of membrane fragments was obtained. The preparation is highly active as a receptor for the bacteriophage T5. The active particles are homogeneous in size with a molecular weight of 230,000 daltons.
D001426:Bacterial Proteins / Q000302:isolation & purification; D002848:Chromatography, DEAE-Cellulose / Q000379:methods; D002852:Chromatography, Ion Exchange / Q000379:methods; D004926:Escherichia coli / Q000032:analysis*; D017830:Octoxynol; D011092:Polyethylene Glycols; D011991:Receptors, Virus / Q000302:isolation & purification*; D013696:Temperature
D001426:Bacterial Proteins; D011991:Receptors, Virus; D011092:Polyethylene Glycols; D017830:Octoxynol