High level of tyrosine protein kinase in a murine lymphoma cell line induced by Moloney leukemia virus.

摘要: Several sarcoma-inducing viruses encode protein kinases that phosphorylate tyrosine residues. Such enzymatic activities can be detected within the detergent-insoluble matrix of transformed fibroblasts. We have analysed kinase in two murine lymphoma cell lines ( MBL2 and LSTRA) induced by Moloney leukemia virus (Mo-MuLV). After incubation these cells with [gamma-32P]ATP, several alkali-resistant phosphoproteins, including a very heavily labelled 55 000 mol. wt. p55 ), been LSTRA, reflecting activity specific to this line. This shares some distinctive properties transforming viruses, i.e., specificity for residues, association membranous and/or cytoskeletal structures, inhibition synthetic peptide derived from phosphorylation site pp60src. In view absence gene MoMuLV , it is likely high level LSTRA line arises expression cellular gene.