title: An improved purification of lactose permease.
abstract: The integral membrane protein lactose permease of Escherichia coli was purified to homogeneity in detergent micelles. No other proteins could be detected in the final product. The molar ratio of lactose permease to lipid was less than 0.2 in detergent solution, thus the preparation was essentially lipid-free. All molecules were functionally active as shown by substrate binding.
mesh_terms: D002462:Cell Membrane / Q000201:enzymology; D002852:Chromatography, Ion Exchange; D004134:Dimyristoylphosphatidylcholine; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins; D026901:Membrane Transport Proteins / Q000302:isolation & purification*; D009004:Monosaccharide Transport Proteins; D010714:Phosphatidylethanolamines; D027981:Symporters
chemical_list: D029968:Escherichia coli Proteins; C050221:LacY protein, E coli; D026901:Membrane Transport Proteins; D009004:Monosaccharide Transport Proteins; D010714:Phosphatidylethanolamines; D027981:Symporters; C007510:1,2-dipalmitoyl-3-phosphatidylethanolamine; C021499:lactose permease; D004134:Dimyristoylphosphatidylcholine