1999
Affinity interaction of hydroxypyruvate reductase from Methylophilus spp. with Cibacron blue F3GA-derived poly(HEMA EGDMA) microspheres: partial purification and characterization
Arica M, Halıcıgil C, Alaeddinoğlu G, Denizli A. Affinity interaction of hydroxypyruvate reductase from Methylophilus spp. with Cibacron blue F3GA-derived poly(HEMA EGDMA) microspheres: partial purification and characterization. Process Biochemistry 1999, 34: 375-381. DOI: 10.1016/s0032-9592(98)00104-6.Peer-Reviewed Original ResearchCibacron Blue F3GABiomimetic dyesAdsorption mediumDimer structureMolecular massNADH solutionAffinity interactionHydroxypyruvate reductaseMicrospheresAbsorption capacityMethylophilus sppSDS-polyacrylamide gelsPartial purificationOptimal pHReductasePolyacrylamideDyeMaximum enzyme activityGelKm valuesPurificationMMPHEnzymeCharacterizationPurification of serine racemase: Biosynthesis of the neuromodulator d-serine
Wolosker H, Sheth K, Takahashi M, Mothet J, Brady R, Ferris C, Snyder S. Purification of serine racemase: Biosynthesis of the neuromodulator d-serine. Proceedings Of The National Academy Of Sciences Of The United States Of America 1999, 96: 721-725. PMID: 9892700, PMCID: PMC15203, DOI: 10.1073/pnas.96.2.721.Peer-Reviewed Original ResearchConceptsBiosynthetic pathwayD-serine occursSerine racemaseAmino acidsD-serineMammalian brainNeuromodulator D-serineL-serineMolecular massSoluble enzymeEndogenous ligandPyridoxal phosphateRat brainN-methyl-D-aspartate receptorsEnzymeKm valuesRacemasePathwayHigh levelsRat cerebral cortexAspartate glutamate receptorsGlutamate receptorsRacemasesType II astrocytesGlial cultures
1977
Suppression of a defective alanyl-tRNA synthetase in Escherichia coli: A compensatory mutation to high alanine affinity
Theall G, Low K, Söll D. Suppression of a defective alanyl-tRNA synthetase in Escherichia coli: A compensatory mutation to high alanine affinity. Molecular Genetics And Genomics 1977, 156: 221-227. PMID: 340903, DOI: 10.1007/bf00283495.Peer-Reviewed Original ResearchConceptsTemperature-resistant revertantsAlanyl-tRNA synthetaseResistant revertantsE. coli mapWild-type enzymeRibosomal proteinsStructural geneGene mapsSynthetase mutantsMutant enzymesParental enzymeCompensatory mutationsTemperature-sensitive characterEscherichia coliAdditional mutationsEnzymeRevertantsSynthetaseMutationsKm valuesAlanineRecAMutantsGenesAffinity
1972
Glutamyl Transfer Ribonucleic Acid Synthetase of Escherichia coli II. INTERACTION WITH INTACT GLUTAMYL TRANSFER RIBONUCLEIC ACID
Lapointe J, Söll D. Glutamyl Transfer Ribonucleic Acid Synthetase of Escherichia coli II. INTERACTION WITH INTACT GLUTAMYL TRANSFER RIBONUCLEIC ACID. Journal Of Biological Chemistry 1972, 247: 4975-4981. PMID: 4341532, DOI: 10.1016/s0021-9258(19)44926-0.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmino Acyl-tRNA SynthetasesCarbon IsotopesCatalysisCentrifugation, Density GradientDiphosphatesDrug StabilityEscherichia coliGlutamatesHot TemperatureHydrogen-Ion ConcentrationKineticsLeucineMagnesiumPhosphorus IsotopesProtein BindingRNA, TransferSpectrometry, FluorescenceValineConceptsGlutamyl-transfer ribonucleic acid synthetaseEscherichia coli IITransfer ribonucleic acidTRNA-GluTRNA-ValTRNA-LeuCognate tRNABiological specificityRibonucleic acidPure enzymeEnzymeSimilar Km valuesComplex formationGradient centrifugationSynthetaseKm valuesFluorescence-quenching studiesTRNAIsoacceptorsComplexesFluorescence quenching studiesHeat inactivationInactivationLeuGluGlutamyl Transfer Ribonucleic Acid Synthetase of Escherichia coli III. INFLUENCE OF THE 46K PROTEIN ON THE AFFINITY OF THE 56K GLUTAMYL TRANSFER RIBONUCLEIC ACID SYNTHETASE FOR ITS SUBSTRATES
Lapointe J, Söll D. Glutamyl Transfer Ribonucleic Acid Synthetase of Escherichia coli III. INFLUENCE OF THE 46K PROTEIN ON THE AFFINITY OF THE 56K GLUTAMYL TRANSFER RIBONUCLEIC ACID SYNTHETASE FOR ITS SUBSTRATES. Journal Of Biological Chemistry 1972, 247: 4982-4985. PMID: 4560497, DOI: 10.1016/s0021-9258(19)44927-2.Peer-Reviewed Original Research
1971
A Comparative Study of the Interactions of Escherichia coli Leucyl-, Seryl-, and Valyl-Transfer Ribonucleic Acid Synthetases with Their Cognate Transfer Ribonucleic Acids
Myers G, Blank H, Söll D. A Comparative Study of the Interactions of Escherichia coli Leucyl-, Seryl-, and Valyl-Transfer Ribonucleic Acid Synthetases with Their Cognate Transfer Ribonucleic Acids. Journal Of Biological Chemistry 1971, 246: 4955-4964. PMID: 4936720, DOI: 10.1016/s0021-9258(18)61956-8.Peer-Reviewed Original ResearchConceptsEscherichia coli KSeryl-tRNA synthetaseLeucyl-tRNA synthetaseRibonucleic acidTransfer ribonucleic acidValyl-tRNA synthetaseTRNA recognitionColi KSynthetase-tRNA complexIsoacceptorsAmino acidsEquilibrium binding studiesPing-pong typeTRNASynthetaseEnzymeKm valuesSubstrate inhibitionBasic similaritiesBinding studiesSerylAcidATPSame bufferSequence
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