TY - JOUR
T1 - Partial amino-terminal sequences of the polyoma nonhistone proteins VP1, VP2, and VP3 synthesized in vitro
AU - Hewick, R. M.
AU - Mellor, A.
AU - Smith, A. E.
AU - Waterfield, M. D.
PY - 1980
Y1 - 1980
N2 - 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. 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.
AB - 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. 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.
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U2 - 10.1128/jvi.33.2.631-636.1980
DO - 10.1128/jvi.33.2.631-636.1980
M3 - Article
C2 - 6251238
AN - SCOPUS:0018842294
SN - 0022-538X
VL - 33
SP - 631
EP - 636
JO - Journal of Virology
JF - Journal of Virology
IS - 2
ER -