The receptor for colicin E3. Isolation and some properties.
A simple method for the isolation of the colicin E3 receptor is described. The receptor was extracted with lithium diiodesalicylate/urea/Triton X-100/EDTA from the cell envelope of Escherichia coli. The combination of affinity chromatography on immobilized protein A of colicin E3 with the efficient extraction led to the preparation of the receptor in a pure form, with a good yield (70%) and high activity. The purified receptor was a pure protein with a molecular weight of 60,000. The receptor protein was prepared in micelles of Triton X-100, and formed an equimolar complex with each E colicin (E1, E2, and E3), respectively. However, in the absence of the micelles, the receptor protein was easily inactivated.
D002462:Cell Membrane / Q000187:drug effects / Q000378:metabolism; D003087:Colicins / Q000378:metabolism; D003090:Coliphages / Q000502:physiology; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins; D007700:Kinetics; D011956:Receptors, Cell Surface; D011971:Receptors, Immunologic / Q000302:isolation & purification* / Q000378:metabolism; D014805:Vitamin B 12 / Q000494:pharmacology
D003087:Colicins; D029968:Escherichia coli Proteins; D011956:Receptors, Cell Surface; D011971:Receptors, Immunologic; C028593:colicin receptor, E coli; D014805:Vitamin B 12