Autographa californica nuclear polyhedrosis virus structural proteins compared from in vivo and in vitro sources.
Polyhedrin obtained from Autographa californica nuclear polyhedrosis virus (AcMNPV) was apparently not modified in terms of primary structure after passage through alternate host systems, both in vivo and in vitro, as investigated by two-dimensional, high-voltage electrophoresis of tryptic digests of this protein as well as amino acid analysis. N-terminal analyses were conducted using an improved technique which showed proline to be the N-terminal amino acid. In addition, passage of enveloped nucleocapsids through alternate hosts as studied by SDS-PAGE showed the polypeptide compositions to be very similar.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002460:Cell Line; D004591:Electrophoresis, Polyacrylamide Gel; D007304:Insect Viruses / Q000032:analysis* / Q000254:growth & development; D007313:Insecta / Q000382:microbiology*; D007814:Larva / Q000382:microbiology; D008970:Molecular Weight; D010455:Peptides / Q000032:analysis; D014764:Viral Proteins / Q000032:analysis*
D000596:Amino Acids; D010455:Peptides; D014764:Viral Proteins