ACTIVE TRANSPORT IN ISOLATED BACTERIAL MEMBRANE VESICLES: BINDING OF β‐GALACTOSIDES TO THE LAC CARRIER PROTEIN
Kaback H, Rudnick G, Schuldiner S, Short S. ACTIVE TRANSPORT IN ISOLATED BACTERIAL MEMBRANE VESICLES: BINDING OF β‐GALACTOSIDES TO THE LAC CARRIER PROTEIN. Annals Of The New York Academy Of Sciences 1975, 264: 350-357. PMID: 769642, DOI: 10.1111/j.1749-6632.1975.tb31495.x.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsPhotoinactivation of the beta-galactoside transport system in Escherichia coli membrane vesicles with an impermeant azidophenylgalactoside.
Rudnick G, Kaback H. Photoinactivation of the beta-galactoside transport system in Escherichia coli membrane vesicles with an impermeant azidophenylgalactoside. Journal Of Biological Chemistry 1975, 250: 6847-6851. PMID: 1099095, DOI: 10.1016/s0021-9258(19)41009-0.Peer-Reviewed Original ResearchPhotoinactivation of the beta-galactoside transport system in Escherichia coli membrane vesicles with 2-nitro-4-azidophenyl-1-thio-beta-D-galactopyranoside.
Rudnick G, Kaback H, Weil R. Photoinactivation of the beta-galactoside transport system in Escherichia coli membrane vesicles with 2-nitro-4-azidophenyl-1-thio-beta-D-galactopyranoside. Journal Of Biological Chemistry 1975, 250: 1371-1375. PMID: 1089657, DOI: 10.1016/s0021-9258(19)41823-1.Peer-Reviewed Original ResearchConceptsMembrane vesiclesBeta-galactoside transport systemEscherichia coli membrane vesiclesEscherichia coli ML 308Lac carrier proteinD-lactateAmino acid transportTransport systemSteady-state levelsML 308Lactose transportAcid transportCarrier proteinVesiclesD-galactopyranosideApparent KmCompetitive inhibitor