1993
Molecular cloning and immunological characterization of the gamma polypeptide, a small protein associated with the Na,K-ATPase.
Mercer R, Biemesderfer D, Bliss D, Collins J, Forbush B. Molecular cloning and immunological characterization of the gamma polypeptide, a small protein associated with the Na,K-ATPase. Journal Of Cell Biology 1993, 121: 579-586. PMID: 8387529, PMCID: PMC2119561, DOI: 10.1083/jcb.121.3.579.Peer-Reviewed Original ResearchConceptsNa,K-ATPaseGamma subunitK-ATPaseSmall membrane proteinsN-linked glycosylationTissue-specific fashionCardiac glycoside bindingGamma subunit mRNAGamma-specific antibodiesNorthern blot analysisHydropathy analysisSequenced proteinsNAB-ouabainMembrane proteinsGamma polypeptidesMolecular cloningGlycoside bindingSmall proteinsNephron segmentsBeta subunitSubunit mRNAAlpha subunitSubunitAmino acidsHydrophobic domains
1984
An apparatus for rapid kinetic analysis of isotopic efflux from membrane vesicles and of ligand dissociation from membrane proteins
Forbush B. An apparatus for rapid kinetic analysis of isotopic efflux from membrane vesicles and of ligand dissociation from membrane proteins. Analytical Biochemistry 1984, 140: 495-505. PMID: 6091496, DOI: 10.1016/0003-2697(84)90200-8.Peer-Reviewed Original Research
1983
Assay of Na,K-ATPase in plasma membrane preparations: Increasing the permeability of membrane vesicles using sodium dodecyl sulfate buffered with bovine serum albumin
Forbush B. Assay of Na,K-ATPase in plasma membrane preparations: Increasing the permeability of membrane vesicles using sodium dodecyl sulfate buffered with bovine serum albumin. Analytical Biochemistry 1983, 128: 159-163. PMID: 6303151, DOI: 10.1016/0003-2697(83)90356-1.Peer-Reviewed Original ResearchConceptsMaximal Na,K-ATPase activityAmount of membrane proteinNa,K-ATPase activityElectric organ of eelIsolated plasma membranesNa,K-ATPaseSodium dodecyl sulfate bufferK-ATPase activityPlasma membrane preparationsTransmembrane proteinsMembrane proteinsDetergent bufferPlasma membraneOptimal activityActivity of membranesBovine serum albuminMembrane vesiclesK-ATPasePermeability of membrane vesiclesDetergentDetergent activitySulfate bufferProteinVesicular natureSerum albumin
1982
Characterization of right-side-out membrane vesicles rich in (Na,K)-ATPase and isolated from dog kidney outer medulla.
Forbush B. Characterization of right-side-out membrane vesicles rich in (Na,K)-ATPase and isolated from dog kidney outer medulla. Journal Of Biological Chemistry 1982, 257: 12678-12684. PMID: 6290476, DOI: 10.1016/s0021-9258(18)33564-6.Peer-Reviewed Original ResearchConceptsDog kidney outer medullaK)-ATPase activityK)-ATPaseKidney outer medullaOuter medullaRight-side-out membrane vesiclesMembrane vesiclesBasolateral membranePorcine trypsinMg2+ + ATPRight-side-out orientationDensity gradient centrifugationCaged ATPIntravesicular volumePresence of Na+H1 populationMedullaMembrane proteinsSucrose gradientsGradient centrifugationTrypsin-sensitiveDetergent treatmentVesicle volumeVesiclesATP