title: Partial amino-terminal sequences of the polyoma nonhistone proteins VP1, VP2, and VP3 synthesized in vitro.
abstract: The three polyoma virus capsid proteins VP1, VP2, and VP3 were synthesized in vitro in the presence of several radiolabeled amino acids and, after purification on sodium dodecyl sulfate-polyacrylamide gels, were subjected to sequential Edman degradation. The partial amino-terminal amino acid sequences obtained were compared with the sequence of amino acids predicted from the polyoma virus DNA sequencing (Arrand et al., J. Virol. 33:606--618, 1980). Together, these results showed that the 5' ends of the VP1, VP2, and VP3 coding sequences are located 1,217, 289, and 634 nucleotides, respectively, from the junction of HpaII restriction fragments 3 and 5.
mesh_terms: D000595:Amino Acid Sequence; D002213:Capsid / Q000235:genetics*; D002474:Cell-Free System; D004591:Electrophoresis, Polyacrylamide Gel; D011120:Polyomavirus / Q000235:genetics*; D014764:Viral Proteins / Q000235:genetics*
chemical_list: D014764:Viral Proteins