Phosphorylation of acidic ribosomal proteins from rabbit reticulocytes by a ribosome-associated casein kinase

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Abstract

Two acidic proteins from 80-S ribosomes were isolated and purified to homogeneity. The purified acidic proteins could be phosphorylated by casein kinase using [gamma-32P]ATP and [gamma-32P]GTP as a phosphoryl donor. The proteins became phosphorylated in situ, too. Sodium dodecyl sulfate polyacrylamide gel analysis of the purified acidic proteins and 80-S particles showed identical phosphoproteins in the 16 000 dalton region.
Original languageEnglish
JournalBBA General Subjects
Volume477
Issue number2
Pages (from-to)185-189
Number of pages4
ISSN0304-4165
Publication statusPublished - 15. Jul 1977

Keywords

  • Adenosine Triphosphate
  • Animals
  • Caseins
  • Guanosine Triphosphate
  • Molecular Weight
  • Protein Kinases
  • Rabbits
  • Reticulocytes
  • Ribosomal Proteins
  • Ribosomes

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