Purification of the MglC/E membrane proteins of the binding protein‐dependent galactose transport system of Salmonella typhimurium

FEBS Letters

Kohiyama, Masamichi¹  Richarme, Gilbert¹ 

[1] Biochimie Génétique, Institut Jacques Monod, Université Paris 7, 2 place Jussieu, 75251 Paris Cedex 05, France

关键词: Binding protein-dependent transport;    Membrane protein;    Proteoliposome;    CHAPS;    (3-(3-Cholamidopropyl)-dimethylammonio)-1 -propanesulfonate);   

DOI  :  10.1016/0014-5793(92)80611-J

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The high affinity galactose transport system of consists of Salmonella typhimurium consists of four proteins, a periplasmic galactose binding protein (the MglB protein), and three inner membrane-associated proteins, the MglA, MglC and MglE proteins. We purified the MglC/E proteins from an MglC/E hyperproducing strain after solubilisation of inclusion bodies in guanidine hydrochloride followed by renaturation in a detergent-containing buffer and affinity chromatography on a MglB—Sepharose column. The MglC/E proteins are devoid of ATPase activity and they complement an extract from a strain carrying a plasmid with the mglA gene for reconstitution of the MglB-dependent galactose transport in proteoliposomes.

【 授权许可】

Unknown