2000
Enhanced Electron Flux and Reduced Calmodulin Dissociation May Explain “Calcium-independent” eNOS Activation by Phosphorylation*
McCabe T, Fulton D, Roman L, Sessa W. Enhanced Electron Flux and Reduced Calmodulin Dissociation May Explain “Calcium-independent” eNOS Activation by Phosphorylation*. Journal Of Biological Chemistry 2000, 275: 6123-6128. PMID: 10692402, DOI: 10.1074/jbc.275.9.6123.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalciumCalmodulinCattleDimerizationEgtazic AcidElectronsEnzyme ActivationKineticsMutationNADH DehydrogenaseNADPNitric OxideNitric Oxide SynthaseNitric Oxide Synthase Type IIIPhosphorylationProtein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-aktStatic ElectricityConceptsSerine 1179Reductase domainCalmodulin dissociationProtein kinase AktWild-type eNOSBovine endothelial nitric oxide synthaseEndothelial nitric oxide synthaseKinase AktRate-limiting stepReductase activityPhosphorylationENOS activationNOS functionPotential mechanismsAspartateENOS catalytic activityENOS activityCytochrome c reductionAktCalmodulinDomainProteinMutationsProductionActivity
1996
Characterization of Bovine Endothelial Nitric Oxide Synthase Expressed inE. coli
Martasek P, Liu Q, Liu J, Roman L, Gross S, Sessa W, Masters B. Characterization of Bovine Endothelial Nitric Oxide Synthase Expressed inE. coli. Biochemical And Biophysical Research Communications 1996, 219: 359-365. PMID: 8604992, DOI: 10.1006/bbrc.1996.0238.Peer-Reviewed Original ResearchConceptsE. coliBaculovirus expression systemBovine endothelial nitric oxide synthaseSDS/PAGEHEK-293 cellsChaperonin GroELHeterologous expressionRecombinant enzymeExpression systemExpression vectorActive enzymeFormation assaysEnzymatic activityColiEnzymeTissue sourcesEndothelial constitutive nitric oxide synthaseProteinSingle bandSynthaseNitric oxide synthaseAbsorbance maximumEndothelial nitric oxide synthase