1994
Alternatively spliced isoforms of the putative renal Na-K-Cl cotransporter are differentially distributed within the rabbit kidney.
Payne J, Forbush B. Alternatively spliced isoforms of the putative renal Na-K-Cl cotransporter are differentially distributed within the rabbit kidney. Proceedings Of The National Academy Of Sciences Of The United States Of America 1994, 91: 4544-4548. PMID: 7514306, PMCID: PMC43822, DOI: 10.1073/pnas.91.10.4544.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingAmino Acid SequenceAnimalsBase SequenceBlotting, NorthernCarrier ProteinsCloning, MolecularColonConserved SequenceDogfishGene LibraryHumansKidneyKidney CortexKidney MedullaMembrane ProteinsMolecular Sequence DataOpen Reading FramesPoly ARabbitsRNARNA, MessengerSalt GlandSequence Homology, Amino AcidSodium-Potassium-Chloride SymportersTranscription, GeneticConceptsNa-K-Cl cotransporterNorthern blot analysisRabbit kidney cDNA libraryRenal Na-K-Cl cotransporterC-terminal cytoplasmic domainC-terminal cytoplasmic regionConsensus splice acceptor siteKidney cDNA libraryAmino acid hydropathySplice acceptor siteBlot analysisN-linked glycosylationRegions of divergenceIntronic DNACDNA clonesCassette exonsCDNA libraryProtein kinase ACytoplasmic domainSpliced isoformsTransmembrane helicesCDNA probeCytoplasmic regionHomologous variantMultiple clones
1991
[3H]bumetanide binding to mouse kidney membranes: identification of corresponding membrane proteins
Haas M, Dunham P, Forbush B. [3H]bumetanide binding to mouse kidney membranes: identification of corresponding membrane proteins. American Journal Of Physiology 1991, 260: c791-c804. PMID: 2018111, DOI: 10.1152/ajpcell.1991.260.4.c791.Peer-Reviewed Original ResearchMeSH KeywordsAffinity LabelsAnimalsBenzophenonesBumetanideCarcinoma, Ehrlich TumorCarrier ProteinsCell FractionationCell MembraneCentrifugation, Density GradientFemaleKidneyKidney CortexKidney MedullaKineticsMembrane ProteinsMiceProtein BindingSodium-Potassium-Chloride SymportersSulfanilamidesTritiumConceptsMouse kidney membranesKidney membranesNa-K-Cl cotransport systemNa-K-ClLow-affinity peakDog kidney membraneMouse Ehrlich ascites tumor cellsMouse kidney proteinsDog kidneyCrude plasma membranesTumor cellsWestern blot analysisEhrlich ascites tumor cellsCotransport systemAscites tumor cellsMouse kidneyMiceStaining profileLow-affinity sitesWestern blottingBinding sitesAntiserum cross-reactedKidneyBlot analysisKidney proteins
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
[3H]bumetanide binding to membranes isolated from dog kidney outer medulla. Relationship to the Na,K,Cl co-transport system.
Forbush B, Palfrey H. [3H]bumetanide binding to membranes isolated from dog kidney outer medulla. Relationship to the Na,K,Cl co-transport system. Journal Of Biological Chemistry 1983, 258: 11787-11792. PMID: 6619143, DOI: 10.1016/s0021-9258(17)44299-2.Peer-Reviewed Original ResearchConceptsOuter medullaCl- co-transport systemDog kidney outer medullaCl- cotransport systemLoop of HenleCo-transport systemLoop diureticsBasolateral membraneKidney outer medullaProximal tubulesAscending limbLuminal membraneCotransport systemKidney cortexMedullaKidney membranesBrush borderCo-transportCrude membranesKidneyDog kidneyBinding to membranesBinding activityGradient centrifugation
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 ResearchMeSH KeywordsAnimalsCell MembraneDogsKidney MedullaKineticsSodium Dodecyl SulfateSodium-Potassium-Exchanging ATPaseTrypsinValinomycinConceptsDog 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 volumeVesiclesATPPurification and characterization of an (Na++K+)-ATPase proteolipid labeled with a photoaffinity derivative of ouabain
Collins J, Forbush B, Lane L, Ling E, Schwartz A, Zot A. Purification and characterization of an (Na++K+)-ATPase proteolipid labeled with a photoaffinity derivative of ouabain. Biochimica Et Biophysica Acta 1982, 686: 7-12. PMID: 6279154, DOI: 10.1016/0005-2736(82)90145-6.Peer-Reviewed Original Research
1979
Evidence that ouabain binds to the same large polypeptide chain of dimeric Na,K-ATPase that is phosphorylated from Pi.
Forbush B, Hoffman J. Evidence that ouabain binds to the same large polypeptide chain of dimeric Na,K-ATPase that is phosphorylated from Pi. Biochemistry 1979, 18: 2308-15. PMID: 221003, DOI: 10.1021/bi00578a027.Peer-Reviewed Original Research
1978
Characterization of a new photoaffinity derivative of ouabain: labeling of the large polypeptide and of a proteolipid component of the Na, K-ATPase.
Forbush B, Kaplan J, Hoffman J. Characterization of a new photoaffinity derivative of ouabain: labeling of the large polypeptide and of a proteolipid component of the Na, K-ATPase. Biochemistry 1978, 17: 3667-76. PMID: 210802, DOI: 10.1021/bi00610a037.Peer-Reviewed Original ResearchRapid photolytic release of adenosine 5'-triphosphate from a protected analogue: utilization by the Na:K pump of human red blood cell ghosts.
Kaplan J, Forbush B, Hoffman J. Rapid photolytic release of adenosine 5'-triphosphate from a protected analogue: utilization by the Na:K pump of human red blood cell ghosts. Biochemistry 1978, 17: 1929-35. PMID: 148906, DOI: 10.1021/bi00603a020.Peer-Reviewed Original Research