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Virology ; 189(1): 320-3, 1992 Jul.
Article in English | MEDLINE | ID: mdl-1604817

ABSTRACT

The amino acid sequence of Agrotis segetum Granulosis virus (AsGV) granulin and A. Segetum nuclear polyhedrosis virus (AsNPV) polyhedrin was determined by sequencing tryptic and chymotryptic peptides from reduced and carboxymethylated proteins and tryptic fragments of oxidized and maleylated granulin. The comparison of the established peptide structures with the primary structures of other occlusion body proteins from related baculoviruses was also used for the polypeptide chains' reconstruction. The polypeptide chains of AsGV granulin and AsNPV polyhedrin comprise 247 and 246 amino acid residues, respectively. The proteins possess a high percentage of homology in their primary structures (63%).


Subject(s)
Baculoviridae/chemistry , Inclusion Bodies, Viral/chemistry , Moths/microbiology , Amino Acid Sequence , Animals , Molecular Sequence Data , Occlusion Body Matrix Proteins , Peptide Fragments/chemistry , Sequence Homology, Nucleic Acid , Viral Structural Proteins
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