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In vitro Cleavage of Pr65^gag by the Moloney Murine Leukaemia Virus Proteolytic Activity Yields p30 whose NH₂-Terminal Sequence Is Identical to Virion p30

Ronald B. Luftig^1,

¹ Department of Microbiology and Immunology, University of South Carolina, School of Medicine, Columbus, South Carolina 29208
and² LBI Basic Research Program, National Cancer Institute, Frederick Cancer Research Facility, P.O. Box B, Frederick, Maryland 21701, U.S.A.

In vitro cleavage of Gazdar murine sarcoma virus Pr65^gag, which has all of the antigenic determinants of Moloney murine leukaemia virus Pr65^gag, 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 Pr65^gag were used to generate the cleaved p30.

Keywords: MuLV, proteolytic cleavage, virion protease

Present address: Department of Microbiology and Immunology, LSU Medical Center, 1901 Perdido Street, New Orleans, Louisiana 70112, U.S.A.

Received 7 August 1984; accepted 19 October 1984.