Inhibition of DNA binding of purified p55v-myc in vitro by antibodies against bacterially expressed myc protein and a synthetic peptide.

摘要: To identify viral myc proteins, we have prepared myc-specific antibodies: (i) against a synthetic peptide corresponding to the nine carboxy-terminal amino acids of (C9); (ii) bacterially expressed protein obtained by inserting SalI-BamHI fragment MC29 DNA clone in expression vector pPLc24. Both antisera recognize 55 000 mol. wt., p55v-myc, MH2- and OK10-transformed fibroblasts. The is located nucleus, as shown indirect immunofluorescence cell fractionation. Antibodies C9 were used purify p55v-myc immunoaffinity column purification (3000-fold) from OK10- MH2-transformed binds double-stranded vitro does p110gag-myc. binding inhibited immunoglobulin fraction antibodies protein. Furthermore, consisting 16 (C16) was isolate specific immunoglobulins which also inhibit vitro. OK10 codes, addition for p200gag-pol-myc polyprotein. majority this cytoplasm (79%). purified single-stranded RNA vitro, unlike other gag-myc or proteins.