Literature DB >> 187238

Characterization of a protein kinase-phosphoprotein system in free cytoplasmic ribonucleoprotein particles of plasma cell tumours.

J M Egly, M Schmitt, J Kempf.   

Abstract

A protein kinase, associated with free cytoplasmic ribonucleoprotein particles (free dRNP) has been purified from mouse plasma cell tumours. This protein kinase is able to phosphorylate in vitro endogenous protein from free dRNP. Some characteristics of this protein kinase have been studied. This protein kinase behaves as being cyclic AMP independent. The properties of this protein kinase were compared with other protein kinases: soluble, ribosome-bound, and nuclear protein kinases. Although there are minor differences it is very similar to a ribosome-associated protein kinase from the plasma cell tumours.

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Year:  1976        PMID: 187238     DOI: 10.1016/0005-2787(76)90280-x

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  3 in total

1.  mRNP proteins, initiation factors and phosphorylation.

Authors:  J M Egly; R Elkaim; M Pierre
Journal:  Mol Biol Rep       Date:  1979-05-31       Impact factor: 2.316

Review 2.  Regulation of mRNA polyadenylation-deadenylation.

Authors:  C M Tsiapalis
Journal:  Mol Biol Rep       Date:  1987       Impact factor: 2.316

3.  In vitro translation studies of the cytoplasmic nonpolysomal particles containing messenger RNA.

Authors:  J P Liautard; J M Egly
Journal:  Nucleic Acids Res       Date:  1980-04-25       Impact factor: 16.971

  3 in total

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