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January 1, 1985Biochemistry

Functional and immunochemical characterization of a mutant of Escherichia coli energy uncoupled for lactose transport

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Authors

DHDoris HerzlingerCornell UniversityNCNancy CarrascoVanderbilt UniversityHKH. Ronald KabackUniversity of California, Los Angeles

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Cite This Study

Herzlinger et al. (1985) studied this question.

synapsesocial.com/papers/6a0d9db3cae7912d2fa5203ehttps://doi.org/10.1021/bi00322a032
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Purified reconstituted lac carrier protein from Escherichia coli is fully functional.1984 · 87 citations
  2. 2Functional molecular weight of the lac carrier protein from Escherichia coli as studied by radiation inactivation analysis.1984 · 37 citations
  3. 3Sidedness of native membrane vesicles of Escherichia coli and orientation of the reconstituted lactose :H+ carrier1984 · 78 citations
  4. 4Direct measurement of lactose/proton symport in Escherichia coli membrane vesicles: further evidence for the involvement of a histidine residue(s)1982 · 50 citations
  5. 5Mechanism of lactose translocation in proteoliposomes reconstituted with lac carrier protein purified from Escherichia coli. II. Deuterium solvent isotope effects1983 · 78 citations