Biopolym. Cell. 1991; 7(1):75-82.
Structure and Function of Biopolymers
Determination of complete amino acid sequence of Agrotis segetum nuclear polyhedrosis virus (NPV) polyhedrin and correction of the primary structure of NPV polyhedrons of Galleria mellonella, Porthetria dispar and Bombyx mori
1Kozlov E. A., 1Levitina T. L., 1Gusak N. M., 1Rodnin N. V., 1Atepalikhina S. A., 1Palchykovska L. H.
  1. Institute of Molecular Biology and Genetics, NAS of Ukraine
    150, Akademika Zabolotnoho Str., Kyiv, Ukraine, 03680

Abstract

The complete amino acid sequence of A. segetum nuclear polyhedrosis virus (NPV) polyhedrin was reconstructed as based on the comparison of tryptic peptides of this protein with the known amino acid sequence of B. mori NPV polyhedrin. The previously published primary structures of NPV polyhedrins of G. mellonela, P. dispar and B. mori were correlated by means of studying the corresponding tryptic peptides.

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