Protein kinase from avian myeloblastosis virus.
J Virol, 1978/2;25(2):546-52.
Houts GE, Miyagi M, Ellis C, Beard D, Watson KF, Beard JW
PMID: 24125
Impact factor: 6.549
Abstract
A protein kinase associated with purified virions of avian myeloblastosis BAI strain A was partially purified by ion-exchange chromatography and gel filtration. The transfer 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 = 9.3), and, on the basis of molecular sieving through Sephadex G-200 and velocity sedimentation on glycerol gradient, the protein kinase has a molecular weight of 45,000.
MeSH terms
Adenosine Triphosphate; Avian Leukosis Virus; Avian Myeloblastosis Virus; Carrier Proteins; Cations, Divalent; Drug Stability; Hydrogen-Ion Concentration; Isoelectric Point; Magnesium; Metals; Molecular Weight; Phosphates; Protein Kinases; Temperature
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