title: Partial purification and characterization of the cation-binding protein and megamodulin from E. coli.
abstract: Megamodulin was partially purified from E. coli by the steps of Bio-Gel P-6DG and Sephadex G-100 filtrations, and DEAE-cellulose ion-exchange. It is a heat-stable, trypsin-labile, and acidic protein which appears to be a large molecule in aggregated 'holo' form. In addition, its dissociation into smaller fragments, cation-binding capacity, interaction with basic proteins, and stimulation of megamodulin-dependent protein kinases (M-PK) from rabbit brain or skeletal muscle, were also demonstrated.
mesh_terms: D001426:Bacterial Proteins / Q000302:isolation & purification*; D002352:Carrier Proteins / Q000302:isolation & purification*; D002412:Cations / Q000378:metabolism; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004926:Escherichia coli / Q000032:analysis*; D006358:Hot Temperature; D047908:Intracellular Signaling Peptides and Proteins; D008970:Molecular Weight; D011494:Protein Kinases / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D002352:Carrier Proteins; D002412:Cations; D047908:Intracellular Signaling Peptides and Proteins; C015482:protein kinase modulator; D011494:Protein Kinases