1988
Purification and characterization of PCPP‐260: A Purkinje cell‐enriched cyclic amp‐regulated membrane phosphoprotein of Mr 260,000
Weeks G, Picciotto M, Nairn A, Walaas S, Greengard P. Purification and characterization of PCPP‐260: A Purkinje cell‐enriched cyclic amp‐regulated membrane phosphoprotein of Mr 260,000. Synapse 1988, 2: 89-96. PMID: 2844000, DOI: 10.1002/syn.890020112.Peer-Reviewed Original ResearchConceptsCAMP-dependent protein kinaseMembrane proteinsProtein kinaseN-lauryl sarcosineIntegral membrane proteinsMajor tryptic phosphopeptidesPhosphoamino acid analysisTotal membrane proteinSodium dodecyl sulfate-polyacrylamide gel electrophoresisMembrane phosphoproteinDodecyl sulfate-polyacrylamide gel electrophoresisTryptic phosphopeptidesSulfate-polyacrylamide gel electrophoresisPossible functional roleProminent proteinsAlpha-methyl mannosideParticulate fractionMammalian cerebellumFunctional roleProteinPeptide mappingConcanavalin A-agaroseGel electrophoresisAcid analysisA-agarose
1987
The cyclic nucleotide-dependent phosphorylation of aortic smooth muscle membrane proteins
Parks T, Nairn A, Greengard P, Jamieson J. The cyclic nucleotide-dependent phosphorylation of aortic smooth muscle membrane proteins. Archives Of Biochemistry And Biophysics 1987, 255: 361-371. PMID: 3036005, DOI: 10.1016/0003-9861(87)90404-8.Peer-Reviewed Original ResearchConceptsG-kinaseA-kinaseGs proteinMembrane proteinsCyclic nucleotide-dependent phosphorylationCAMP-dependent protein kinase activityCGMP-dependent protein kinaseKinase catalytic subunitEndogenous A-kinaseProtein kinase activityPeptide mappingTwo-dimensional peptide mappingMembrane-bound formCyclic nucleotidesHigh-salt washMuscle membrane proteinsCatalytic subunitFunctional homologyProtein kinasePhosphorylation stateCytosolic formKinase activitySalt washIntracellular concentrationSoluble form