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Viitanen, P., Garcia, M. L., Kaback, H. R. (1984) Purified reconstituted lac carrier protein from Escherichia coli is fully functional. Proceedings of the National Academy of Sciences, 81 (6) 1629-1633 doi:10.1073/pnas.81.6.1629

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Reference TypeJournal (article/letter/editorial)
TitlePurified reconstituted lac carrier protein from Escherichia coli is fully functional.
JournalProceedings of the National Academy of Sciences
AuthorsViitanen, P.Author
Garcia, M. L.Author
Kaback, H. R.Author
Year1984 (March 1)Volume81
Issue6
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.81.6.1629Search in ResearchGate
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Mindat Ref. ID1439924Long-form Identifiermindat:1:5:1439924:2
GUID0
Full ReferenceViitanen, P., Garcia, M. L., Kaback, H. R. (1984) Purified reconstituted lac carrier protein from Escherichia coli is fully functional. Proceedings of the National Academy of Sciences, 81 (6) 1629-1633 doi:10.1073/pnas.81.6.1629
Plain TextViitanen, P., Garcia, M. L., Kaback, H. R. (1984) Purified reconstituted lac carrier protein from Escherichia coli is fully functional. Proceedings of the National Academy of Sciences, 81 (6) 1629-1633 doi:10.1073/pnas.81.6.1629
In(1984, March) Proceedings of the National Academy of Sciences Vol. 81 (6) Proceedings of the National Academy of Sciences

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Goldkorn, T., Rimon, G., Kempner, E. S., Kaback, H. R. (1984) Functional molecular weight of the lac carrier protein from Escherichia coli as studied by radiation inactivation analysis. Proceedings of the National Academy of Sciences, 81 (4) 1021-1025 doi:10.1073/pnas.81.4.1021
Matsushita, K., Patel, L., Gennis, R. B., Kaback, H. R. (1983) Reconstitution of active transport in proteoliposomes containing cytochrome o oxidase and lac carrier protein purified from Escherichia coli. Proceedings of the National Academy of Sciences, 80 (16) 4889-4893 doi:10.1073/pnas.80.16.4889
Puttner, I. B., Kaback, H. R. (1988) lac permease of Escherichia coli containing a single histidine residue is fully functional. Proceedings of the National Academy of Sciences, 85 (5) 1467-1471 doi:10.1073/pnas.85.5.1467
Carrasco, N., Tahara, S. M., Patel, L., Goldkorn, T., Kaback, H. R. (1982) Preparation, characterization, and properties of monoclonal antibodies against the lac carrier protein from Escherichia coli. Proceedings of the National Academy of Sciences, 79 (22) 6894-6898 doi:10.1073/pnas.79.22.6894
Goldkorn, T., Rimon, G., Kaback, H. R. (1983) Topology of the lac carrier protein in the membrane of Escherichia coli. Proceedings of the National Academy of Sciences, 80 (11) 3322-3326 doi:10.1073/pnas.80.11.3322
Roepe, P. D., Kaback, H. R. (1989) Characterization and functional reconstitution of a soluble form of the hydrophobic membrane protein lac permease from Escherichia coli. Proceedings of the National Academy of Sciences, 86 (16) 6087-6091 doi:10.1073/pnas.86.16.6087
Padan, E., Sarkar, H. K., Viitanen, P. V., Poonian, M. S., Kaback, H. R. (1985) Site-specific mutagenesis of histidine residues in the lac permease of Escherichia coli. Proceedings of the National Academy of Sciences, 82 (20) 6765-6768 doi:10.1073/pnas.82.20.6765
Carrasco, N., Herzlinger, D., Mitchell, R., DeChiara, S., Danho, W., Gabriel, T. F., Kaback, H. R. (1984) Intramolecular dislocation of the COOH terminus of the lac carrier protein in reconstituted proteoliposomes. Proceedings of the National Academy of Sciences, 81 (15) 4672-4676 doi:10.1073/pnas.81.15.4672
Kaczorowski, G. J., LeBlanc, G., Kaback, H. R. (1980) Specific labeling of the lac carrier protein in membrane vesicles of Escherichia coli by a photoaffinity reagent. Proceedings of the National Academy of Sciences, 77 (11) 6319-6323 doi:10.1073/pnas.77.11.6319
(1984) Enzymatic properties of purified Escherichia coli uvrABC proteins. Proceedings of the National Academy of Sciences, 81 (6) 1911 doi:10.1073/pnas.81.6.1911
Therisod, H., Weil, R., Shechter, E. (1978) Functional lac carrier protein in cytoplasmic membrane vesicles isolated from Escherichia coli: Temperature and pH dependence of dansyl-galactoside binding. Proceedings of the National Academy of Sciences, 75 (9) 4214-4218 doi:10.1073/pnas.75.9.4214
 
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