Purification and characterization of the membrane-bound complex of an ABC transporter, the histidine permease

The bacterial histidine permease, an ABC transporter, from Salmonella typhimurium is composed of a membrane-bound complex, HisQMP2, comprising two hydrophobic subunits (HisQ and HisM), two copies of an ATP-hydrolyzing subunit, HisP, and a soluble receptor, HisJ. We describe the purification and char...

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Veröffentlicht in:	Journal of bioenergetics and biomembranes 2001-04, Vol.33 (2), p.79-92
Hauptverfasser:	Ames, G F, Nikaido, K, Wang, I X, Liu, P Q, Liu, C E, Hu, C
Format:	Artikel
Sprache:	eng
Schlagworte:	ABC transporters Adenosine Triphosphatases - chemistry Adenosine Triphosphatases - isolation & purification Adenosine Triphosphatases - metabolism Amino Acid Transport Systems, Basic - chemistry Amino Acid Transport Systems, Basic - isolation & purification Amino Acid Transport Systems, Basic - metabolism ATP ATP-Binding Cassette Transporters - chemistry ATP-Binding Cassette Transporters - isolation & purification ATP-Binding Cassette Transporters - metabolism Bacteria Bacterial Proteins - chemistry Bacterial Proteins - isolation & purification Bacterial Proteins - metabolism Biological Transport, Active Detergents Membranes - chemistry Molecular Weight Permeability Phospholipids - pharmacology Protein Subunits Proteins Proteolipids Salmonella typhimurium - metabolism Solubility
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