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- W2069730901 abstract "In free messenger ribonucleoprotein particles (mRNP) and polysomes from plasmacytoma cells, a phosphorylated protein/protein kinase system has been characterized by a combination of oligo(dT)-cellulose chromatography and CsCl isopycnic gradient centrifugation. The presence phosphorylated in vivo has been detected in both types of particles. Endogenous protein phosphorylation occurs in vitro by particle-associated cAMP-independent protein kinase(s) using [gamma-32P]ATP and [gamma-32P]GTP. These kinases are sensitive to hemin action. Analysis of mRNP proteins by gel electrophoresis and autoradiography showed strong analogies between the phosphorylation patterns obtained in vivo and in vitro, suggesting a substrate specificity for the associated enzymes. The phosphorylated proteins have been compared to initiation factors and ribosomal proteins. We have partially purified the cAMP-independent protein kinase activities responsible for the endogenous phosphorylation in free mRNP and polysomes; two activities were identified in free mRNP whereas three activities were found to be associated with polysomes." @default.
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- W2069730901 date "2005-03-03" @default.
- W2069730901 modified "2023-10-15" @default.
- W2069730901 title "Protein Kinases and Their Protein Substrates in Free Messenger Ribonucleoprotein Particles and Polysomes from Mouse Plasmacytoma Cells" @default.
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- W2069730901 doi "https://doi.org/10.1111/j.1432-1033.1981.tb06413.x" @default.
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