1988
[17] Type II cAMP-dependent protein kinase regulatory subunit-binding proteins
Lohmann S, De Camilli P, Walter U. [17] Type II cAMP-dependent protein kinase regulatory subunit-binding proteins. Methods In Enzymology 1988, 159: 183-193. PMID: 2842584, DOI: 10.1016/0076-6879(88)59019-5.Peer-Reviewed Original ResearchConceptsRII subunitsCytosolic cAMP-dependent protein kinaseAdditional proteinsType II cAMP-dependent proteinCAMP-dependent protein kinaseCAMP-dependent proteinMicrotubule-associated proteinsRII overlayProtein kinaseSDS-polyacrylamide gel electrophoresisCertain proteinsNative stateProteinSteps of purificationGel electrophoresisSubunitsCellular structureAssay conditionsNonspecific interactionsRIIHigh affinityHigh enough affinityLight microscopyKinaseAffinity
1984
The hydrogen ion-pumping adenosine triphosphatase of platelet dense granule membrane. Differences from F1F0- and phosphoenzyme-type ATPases.
Dean G, Fishkes H, Nelson P, Rudnick G. The hydrogen ion-pumping adenosine triphosphatase of platelet dense granule membrane. Differences from F1F0- and phosphoenzyme-type ATPases. Journal Of Biological Chemistry 1984, 259: 9569-9574. PMID: 6204985, DOI: 10.1016/s0021-9258(17)42738-4.Peer-Reviewed Original ResearchConceptsGranule ATPaseGranule membranesMitochondrial membraneATP hydrolysisIon-translocating ATPasesEnergy-transducing membranesDense granule membraneIdentical assay conditionsF1F0-ATPasesSubstrate specificityPlasma membraneMitochondrial ATPaseInhibitor sensitivityATPasesATPaseATPase activityConcentrations of NaN3Cation requirementATPase moleculesMembraneN-ethylmaleimideAssay conditionsAdenosine triphosphataseEfrapeptinOligomycin
1977
Purification and some properties of Escherichia coli tRNA nucleotidyltransferase.
Schofield P, Williams K. Purification and some properties of Escherichia coli tRNA nucleotidyltransferase. Journal Of Biological Chemistry 1977, 252: 5584-5588. PMID: 328503, DOI: 10.1016/s0021-9258(19)63390-9.Peer-Reviewed Original ResearchConceptsTransition metal chelating agentsMetal chelating agentsSodium dodecyl sulfate gel electrophoresisDodecyl sulfate gel electrophoresisSulfate gel electrophoresisTurnover numberChelating agentOverall yieldMolecular weightPure enzymeIsoelectric pointKey stepIdentical isoelectric pointsSephadex chromatographyCrude extractPurificationAffinity columnGel electrophoresisEscherichia coli tRNA nucleotidyltransferaseSpecific activityAssay conditionsChromatographyEnzymeTRNA nucleotidyltransferaseOptimal assay conditions
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