Biopolym. Cell. 1991; 7(1):87-93.
Structure and Function of Biopolymers
Reconstruction of the granulin polypeptide chain of the Agrotis segetum granulosis virus. Complete amino acid sequence
1Rodnin N. V., 1Levitina T. L., 1Gusak N. M., 1Kozlov E. A.
  1. Institute of Molecular Biology and Genetics, NAS of Ukraine
    150, Akademika Zabolotnoho Str., Kyiv, Ukraine, 03680

Abstract

The complete amino acid sequence of the granulin of the A. segetum granulosis virus has been reconstructed using the data on tryptic and chymotryptic peptides of protein. In some cases the peptides obtained are compared with the amino acid sequences of the Trlchoplusia ni and Pirn's brassicae granulosis virus granulins. The polypeptide chain comprises 247 amino acids residues having the molecular weight 29135. The peculiarities of the reconstruction of polypeptide chain and cleavage of granulin by trypsin chymotrypsin and proteinase from granula are discussed.

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