2005
Polymorphisms in Human Organic Anion-transporting Polypeptide 1A2 (OATP1A2) IMPLICATIONS FOR ALTERED DRUG DISPOSITION AND CENTRAL NERVOUS SYSTEM DRUG ENTRY*
Lee W, Glaeser H, Smith LH, Roberts RL, Moeckel GW, Gervasini G, Leake BF, Kim RB. Polymorphisms in Human Organic Anion-transporting Polypeptide 1A2 (OATP1A2) IMPLICATIONS FOR ALTERED DRUG DISPOSITION AND CENTRAL NERVOUS SYSTEM DRUG ENTRY*. Journal Of Biological Chemistry 2005, 280: 9610-9617. PMID: 15632119, DOI: 10.1074/jbc.m411092200.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAmino Acid SubstitutionBrainEnkephalin, D-Penicillamine (2,5)-EstroneHumansKidneyKineticsLiverLiver-Specific Organic Anion Transporter 1Models, MolecularMolecular Sequence DataOligopeptidesOrgan SpecificityPolymorphism, GeneticPolymorphism, Single NucleotideProtein ConformationProtein Structure, SecondaryConceptsTransport activityPlasma membrane expressionCell surface biotinylationBroad substrate specificityGenomic DNA samplesReduced transport activityApparent molecular sizeSingle nucleotide polymorphismsGenetic variationSubstrate specificitySurface biotinylationGlycosylation statusOrganic anion-transporting polypeptide 1A2Substrate-dependent changesNonsynonymous polymorphismsRenal distal nephronMembrane expressionNucleotide polymorphismsG variantDrug uptake transportersSubstrate drugsConfocal microscopyDrug dispositionCentral nervous system entryT variant
1994
Purification of Human and Rat Kidney Aldose Reductase
Moeckel G, Hallbach J, Guder W. Purification of Human and Rat Kidney Aldose Reductase. Enzyme And Protein 1994, 48: 45-50. PMID: 7787970, DOI: 10.1159/000474968.Peer-Reviewed Original ResearchConceptsPurification of humanAldose reductaseRat kidney papillaRat kidney aldose reductaseSubstrate specificityHuman enzymeAffinity chromatographic procedureBlue SepharoseSDS-PAGESimilar molecular weightReductaseEnzymeMolecular weightSingle bandChromatographic procedureSorbitol formationKinetic constantsKidney papillaHuman kidneyHumansInner medulla