Characterization of protein phosphorylation in acetylcholine receptor-enriched membrane preparations from torpedo fuscomaculata

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dc.contributor.authorCarstens M.E.
dc.contributor.authorWeller M.
dc.contributor.authorNeethling A.C.
dc.contributor.authorTaljaard J.J.F.
dc.date.accessioned2011-05-15T16:00:02Z
dc.date.available2011-05-15T16:00:02Z
dc.date.issued1982
dc.description.abstractWhen the acetylcholine receptor (AChR*) from Torpedo is phosphorylated, ATP is found to bind non-covalently to the preparation. After correction is made for this binding of ATP, the phosphorylation reaction has a Km of 0,16 mM, a pH optimum of 8,6 and reaches maximal activity within 3 min. The intrinsic kinase activity is very specific for the AChR and does not phosphorylate either histones or phosvitin. The only amino acid to be phosphorylated is serine and cyclic GMP causes stimulation of the reaction. © 1982 Martinus Nijhoff/Dr W. Junk Publishers.
dc.description.versionArticle
dc.identifier.citationMolecular and Cellular Biochemistry
dc.identifier.citation42
dc.identifier.citation3
dc.identifier.issn3008177
dc.identifier.other10.1007/BF00238510
dc.identifier.urihttp://hdl.handle.net/10019.1/11490
dc.subjectacetylcholine
dc.subjectadenosine triphosphate
dc.subjectcholinergic receptor
dc.subjectcyclic AMP
dc.subjectcyclic GMP
dc.subjectmanganese
dc.subjectphosphotransferase
dc.subjectserine
dc.subjectanimal
dc.subjectarticle
dc.subjectelectric organ
dc.subjectkinetics
dc.subjectmembrane
dc.subjectmetabolism
dc.subjectphosphorylation
dc.subjectTorpedo
dc.subjectAcetylcholine
dc.subjectAdenosine Triphosphate
dc.subjectAnimal
dc.subjectCyclic AMP
dc.subjectCyclic GMP
dc.subjectElectric Organ
dc.subjectKinetics
dc.subjectManganese
dc.subjectMembranes
dc.subjectPhosphorylation
dc.subjectPhosphotransferases
dc.subjectReceptors, Cholinergic
dc.subjectSerine
dc.subjectSupport, Non-U.S. Gov't
dc.subjectTorpedo
dc.titleCharacterization of protein phosphorylation in acetylcholine receptor-enriched membrane preparations from torpedo fuscomaculata
dc.typeArticle
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