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Protein kinase from avian myeloblastosis virus


Protein kinase from avian myeloblastosis virus



Journal of Virology 25(2): 546-552



ISSN/ISBN: 0022-538X

PMID: 24125

A protein kinase associated with purifed virions of avian myeloblastosis BAI strain A was partially purified by ion-exchange chromatography and gel filtration. The tranfer of phosphate catalyzed by this enzyme required a divalent metal ion and ATP as phosphate donor. GTP could not be substituted for ATP, and the reaction was unaffected by either cyclic AMP or beef-heart protein-kinase inhibitor. Of the virus and nonvirus proteins tested as phosphate acceptors, only acidic proteins were phosphorylated. In particular, purified preparations of reverse transcriptase from avian myeloblastosis virus did not accept phosphate. The enzyme is a basic protein (pI [isoelectric point] = 9.3), and, on the basis of molecular sieving through Sephadex G-200 and velocity sedimentation on glycerol gradient, the protein kinase has a MW of 45,000.

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Accession: 000472930

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Related references

Protein kinase and phosphoproteins of avian myeloblastosis virus. Journal of Virology 21(3): 843-848, 1977

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