title: The preparation and biochemical characterization of intact capsids of equine infectious anemia virus.
abstract: Capsids of equine infectious anemia virus have been isolated as cone-shaped particles 60 x 120 nm in size. Detergent treatment of whole virus followed by two cycles of rate-zonal centrifugation in Ficoll produces these capsids in a yield of approximately 10%. The major protein components are the gag-encoded p11 nucleocapsid protein and p26 capsid protein, which are present in equimolar amounts. Substantial cleavage of p11 to p6 and p4 can be observed under conditions where the viral protease packaged in the capsid is enzymatically active.
authors.affiliation: Laboratory of Molecular Virology and Carcinogenesis, NCI-Frederick Cancer Research Facility, Maryland 21701.
authors.forename: M M
authors.initials: MM
authors.lastname: Roberts
authors.forename: S
authors.initials: S
authors.lastname: Oroszlan
mesh_terms: D002213:Capsid / Q000201:enzymology / Q000302:isolation & purification* / Q000648:ultrastructure; D002501:Centrifugation, Zonal; D003902:Detergents; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D004860:Infectious Anemia Virus, Equine / Q000032:analysis* / Q000201:enzymology / Q000648:ultrastructure; D012367:RNA, Viral / Q000302:isolation & purification; D014758:Viral Core Proteins / Q000302:isolation & purification / Q000648:ultrastructure
chemical_list: D003902:Detergents; D012367:RNA, Viral; D014758:Viral Core Proteins