In vitro cleavage of gag-myc fused protein P110 of a defective leukaemia virus MC29 by retroviral protease p15.
Gag-related proteins were precipitated from 35S-methionine-labelled cells of the PR-2 line derived from a hepatoma induced by virus MC29. Immunoprecipitates were incubated with viral protease p15 and the cleavage products of P110 were analysed in SDS-PAGE. The major cleavage fragment of P110 is a protein with mol. wt. of 56 000. Preparative isolation of the non-gag fragments from protein P110 by means of a gag immunosorbent showed that the 56K fragment did not contain any gag specific antigenic determinants. This finding was also confirmed by performing immunization with this fragment. Cleavage of protein P110 and the properties of cleavage products are discussed.
D000818:Animals; D000956:Antigens, Viral / Q000235:genetics* / Q000302:isolation & purification; D016282:Aspartic Acid Endopeptidases; D001354:Avian Leukosis Virus / Q000235:genetics*; D001358:Avian Sarcoma Viruses / Q000201:enzymology*; D002460:Cell Line; D002645:Chickens; D004591:Electrophoresis, Polyacrylamide Gel; D015683:Gene Products, gag; D008114:Liver Neoplasms, Experimental / Q000382:microbiology*; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000378:metabolism*; D014764:Viral Proteins / Q000235:genetics* / Q000302:isolation & purification
D000956:Antigens, Viral; D015683:Gene Products, gag; D014764:Viral Proteins; D010447:Peptide Hydrolases; D016282:Aspartic Acid Endopeptidases; C036946:protease p15