1.
J Bacteriol
; 187(8): 2908-11, 2005 Apr.
Artículo
en Inglés
| MEDLINE
| ID: mdl-15805537
RESUMEN
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.