[Physico-chemical properties of cyclic nucleotide-independent protein kinase from the myxomycete Physarum polycephalum].
Some physico-chemical properties of cyclic nucleotide-independent protein kinase from the myxomycete Physarum polycephalum were studied. The enzyme is not activated by Ca2+ and double-stranded RNA of poly(A)-poly(Y). The nature of the amino acid, target for phosphorylation, for the homogenous enzyme was established by two-dimensional electrophoresis, using casein as a protein substrate. The enzyme exclusively phosphorylates threonine residues in the casein molecule.
D002118:Calcium / Q000494:pharmacology; D004789:Enzyme Activation; D007700:Kinetics; D010804:Physarum / Q000201:enzymology*; D011063:Poly A-U; D011494:Protein Kinases / Q000378:metabolism*
D011063:Poly A-U; D011494:Protein Kinases; D002118:Calcium
Izuchenie nekotorykh fiziko-khimicheskikh svoĭstv tsiklonukleotidnezavisimoĭ proteinkinazy iz miksomitseta Physarum polycephalum.