Functional reassembly of the Escherichia coli maltose transporter following purification of a MalF-MalG subassembly.
نویسندگان
چکیده
Taking advantage of a chaperone-like function of MalK, a stable complex of MalF-MalG could be solubilized from the Escherichia coli membrane and purified in high yield in the absence of MalK. This MalF-MalG complex was competent for efficient reassembly of a functional MalFGK(2) maltose transporter complex both in detergent solution and in proteoliposomes.
منابع مشابه
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عنوان ژورنال:
- Journal of bacteriology
دوره 187 8 شماره
صفحات -
تاریخ انتشار 2005