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PubMed:6229539 JSONTXT 26 Projects

Annnotations TAB TSV DIC JSON TextAE Lectin_function IAV-Glycan

Id Subject Object Predicate Lexical cue
T1 0-102 Sentence denotes Phosphorylation-induced mobility shift in phospholamban in sodium dodecyl sulfate-polyacrylamide gels.
T1 0-102 Sentence denotes Phosphorylation-induced mobility shift in phospholamban in sodium dodecyl sulfate-polyacrylamide gels.
T2 103-195 Sentence denotes Evidence for a protein structure consisting of multiple identical phosphorylatable subunits.
T2 103-195 Sentence denotes Evidence for a protein structure consisting of multiple identical phosphorylatable subunits.
T3 196-405 Sentence denotes Phosphorylation of purified phospholamban isolated from canine cardiac sarcoplasmic reticulum vesicles decreased the electrophoretic mobility of the protein in sodium dodecyl sulfate (SDS)-polyacrylamide gels.
T3 196-405 Sentence denotes Phosphorylation of purified phospholamban isolated from canine cardiac sarcoplasmic reticulum vesicles decreased the electrophoretic mobility of the protein in sodium dodecyl sulfate (SDS)-polyacrylamide gels.
T4 406-531 Sentence denotes Different mobility forms of phospholamban in SDS gels were visualized both by direct protein staining and by autoradiography.
T4 406-531 Sentence denotes Different mobility forms of phospholamban in SDS gels were visualized both by direct protein staining and by autoradiography.
T5 532-744 Sentence denotes Unphosphorylated phospholamban migrated with an apparent Mr = 25,000 in SDS gels; maximal phosphorylation of phospholamban by cAMP- or Ca2+-calmodulin-dependent protein kinase increased the apparent Mr to 27,000.
T5 532-744 Sentence denotes Unphosphorylated phospholamban migrated with an apparent Mr = 25,000 in SDS gels; maximal phosphorylation of phospholamban by cAMP- or Ca2+-calmodulin-dependent protein kinase increased the apparent Mr to 27,000.
T6 745-992 Sentence denotes Partial phosphorylation of phospholamban by either protein kinase gave intermediate mobility forms of molecular weights between 25,000 and 27,000, suggesting that more than one phosphorylation site was present on the holoprotein for each activity.
T6 745-992 Sentence denotes Partial phosphorylation of phospholamban by either protein kinase gave intermediate mobility forms of molecular weights between 25,000 and 27,000, suggesting that more than one phosphorylation site was present on the holoprotein for each activity.
T7 993-1320 Sentence denotes Boiling of phospholamban in SDS dissociated the holoprotein into an apparently homogeneous class of low molecular weight "monomers." Only two mobility forms of monomeric phospholamban were observed in SDS gels after phosphorylation by cAMP-dependent protein kinase, corresponding to 9-kDa dephospho- and 11-kDa phosphoproteins.
T7 993-1320 Sentence denotes Boiling of phospholamban in SDS dissociated the holoprotein into an apparently homogeneous class of low molecular weight "monomers." Only two mobility forms of monomeric phospholamban were observed in SDS gels after phosphorylation by cAMP-dependent protein kinase, corresponding to 9-kDa dephospho- and 11-kDa phosphoproteins.
T8 1321-1537 Sentence denotes All of the 9-kDa protein could be phosphorylated and converted into the 11-kDa mobility form, suggesting the presence of only one site of phosphorylation on a single type of monomer for cAMP-dependent protein kinase.
T8 1321-1537 Sentence denotes All of the 9-kDa protein could be phosphorylated and converted into the 11-kDa mobility form, suggesting the presence of only one site of phosphorylation on a single type of monomer for cAMP-dependent protein kinase.
T9 1538-1819 Sentence denotes Simultaneous phosphorylation of monomeric phospholamban by cAMP-dependent protein kinase and Ca2+-calmodulin-dependent protein kinase gave an additional mobility form of the protein, suggesting that different sites of phosphorylation were present for each activity on each monomer.
T9 1538-1819 Sentence denotes Simultaneous phosphorylation of monomeric phospholamban by cAMP-dependent protein kinase and Ca2+-calmodulin-dependent protein kinase gave an additional mobility form of the protein, suggesting that different sites of phosphorylation were present for each activity on each monomer.
T10 1820-2076 Sentence denotes Incomplete dissociation of the holoprotein by boiling it in a relatively low concentration of SDS facilitated the detection of five major mobility forms of the protein in SDS gels, and the mobilities of all of these forms were decreased by phosphorylation.
T10 1820-2076 Sentence denotes Incomplete dissociation of the holoprotein by boiling it in a relatively low concentration of SDS facilitated the detection of five major mobility forms of the protein in SDS gels, and the mobilities of all of these forms were decreased by phosphorylation.
T11 2077-2359 Sentence denotes We propose that the high molecular weight form of phospholamban is a multimer of electrophoretically indistinguishable monomers, each of which contains a different phosphorylation site for cAMP-dependent protein kinase activity and Ca2+-calmodulin-dependent protein kinase activity.
T11 2077-2359 Sentence denotes We propose that the high molecular weight form of phospholamban is a multimer of electrophoretically indistinguishable monomers, each of which contains a different phosphorylation site for cAMP-dependent protein kinase activity and Ca2+-calmodulin-dependent protein kinase activity.
T12 2360-2512 Sentence denotes Phosphorylation of phospholamban at multiple sites is responsible for the various mobility forms of the holoprotein detected in SDS-polyacrylamide gels.
T12 2360-2512 Sentence denotes Phosphorylation of phospholamban at multiple sites is responsible for the various mobility forms of the holoprotein detected in SDS-polyacrylamide gels.