The DOI matches its Crossref record.
Purification and reconstitution of functional lactose carrier from Escherichia coli.
Open accessAbstract
The lactose carrier protein of Escherichia coli was purified by a simple procedure employing differential solubilization and ion-exchange chromatography and reconstituted into liposomes by octylglucoside dilution. The proteoliposomes exhibited both membrane potential-driven lactose transport and lactose counterflow. Furthermore, the purified protein was identified as the product of the lac y gene. These and other results demonstrate that the lactose carrier is the only polypeptide species essential for energy-coupled lactose transport and counterflow.
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Citations
Cited by
Chen, L.-Q., Cheung, L. S., Feng, L., Tanner, W., & Frommer, W. B. (2015) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060614-033904 · Cited by 507
Taglicht, D., Padan, E., & Schuldiner, S. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)99161-1 · Cited by 271
Metadata
- Authors
- Newman, M. J., Foster, D. L., Wilson, T. H., & Kaback, H. R.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1981-11
- Volume
- 256
- Issue
- 22
- Pages
- 11804-11808
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1784665074
- Cited by
- 311
- References
- 0
- FWCI
- 13.20
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Newman, M. J., Foster, D. L., Wilson, T. H., & Kaback, H. R. (1981). Purification and reconstitution of functional lactose carrier from Escherichia coli. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)68477-2
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
