In vitro cleavage of Pr65gag by the Moloney murine leukaemia virus proteolytic activity yields p30 whose NH2-terminal sequence is identical to virion p30.
In vitro cleavage of Gazdar murine sarcoma virus Pr65gag, which has all of the antigenic determinants of Moloney murine leukaemia virus Pr65gag, i.e. p15, p12, p30 and p10, by the Moloney murine leukaemia virus proteolytic activity yielded a p30 whose partial NH2-terminal sequence was identical to Moloney murine leukaemia virus. Both [3H]leucine-labelled and unlabelled Pr65gag were used to generate the cleaved p30.
Yoshinaka
Y
Y
Shames
R B
RB
Luftig
R B
RB
Smythers
G W
GW
Oroszlan
S
S
D000595:Amino Acid Sequence; D000956:Antigens, Viral / Q000032:analysis; D000939:Epitopes / Q000032:analysis; D015683:Gene Products, gag; D008979:Moloney murine leukemia virus / Q000201:enzymology* / Q000276:immunology; D010447:Peptide Hydrolases / Q000378:metabolism*; D011498:Protein Precursors / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D009053:Sarcoma Viruses, Murine / Q000032:analysis* / Q000276:immunology; D014758:Viral Core Proteins; D014764:Viral Proteins / Q000032:analysis / Q000096:biosynthesis* / Q000276:immunology / Q000378:metabolism*
D000956:Antigens, Viral; D000939:Epitopes; D015683:Gene Products, gag; D011498:Protein Precursors; D014758:Viral Core Proteins; D014764:Viral Proteins; D010447:Peptide Hydrolases