Control of H+/Lactose Coupling by Ionic Interactions in the Lactose Permease ofEscherichia coli
✍ Scribed by J. L. Johnson; R. J. Brooker
- Book ID
- 105926305
- Publisher
- Springer
- Year
- 2004
- Tongue
- English
- Weight
- 231 KB
- Volume
- 198
- Category
- Article
- ISSN
- 0022-2631
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## Abstract Lactose transport in membrane vesicles containing lactose permease with a single Cys residue in place of Val 315 is inactivated by __N__‐ethylmaleimide in a manner that is stimulated by substrate or by a H^+^ electrochemical gradient (δμ, Sahin‐Tóth M, Kaback HR, 1993, __Protein Sci 2__
## Abstract By using a lactose permease mutant containing a single Cys residue in place of Val 331 (helix X), conformational changes induced by ligand binding were studied. With right‐side‐out membrane vesicles containing Val 331 → Cys permease, lactose transport is inactivated by either __N__‐ethy