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
- 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.
Full text: (PDF, in Russian)
References
[1]
Gusak NM, Kozlov EA, Rodnin NV, Serebryany SB. The structure of the tryptic peptides of polyhedrin of the nuclear polyhedrosis virus of Agrotis segetum. Biopolym Cell. 1985; 1(6):312-7.
[2]
Kozlov EA, Levitina TL, Katsman MS, Gusak NM, Serebryany SB. Reconstruction of the polypeptide chain of the inclusion body protein of the silkworm nuclear polyhedrosis virus. Complete amino acid sequence. Russian Journal of Bioorganic Chemistry. 1978; 4(8):1048-53.
[3]
Gusak N. M., Kozlov E. A., Ovander M. N., Serebryany S. B. Tryptic peptides of inclusion body protein of nuclear polyhedrosis virus of Galleria mellonell. Russian Journal of Bioorganic Chemistry. 1981; 7(7):996-1007.
[4]
Gusak N. M., Kozlov E. A., Ovander M. N., Serebryany S. B. Tryptic peptides of inclusion body protein of nuclear polyhedrosis virus of Galleria mellonell. Russian Journal of Bioorganic Chemistry. 1981; 7(7):996-1007.
[5]
Iatrou K, Ito K, Witkiewicz H. Polyhedrin gene of Bombyx mori nuclear polyhedrosis virus. J Virol. 1985;54(2):436-45.
[6]
Smith IR, van Beek NA, Podgwaite JD, Wood HA. Physical map and polyhedrin gene sequence of Lymantria dispar nuclear polyhedrosis virus. Gene. 1988;71(1):97-105.
[7]
Guidotti G. The action of carboxypeptidases A and B on the separated alpha and beta chains of normal adult human hemoglobin. Biochim Biophys Acta. 1960;42:177-9.
[8]
Kozlov EA, Levitina TL, Katsman MS, Gusak NM, Ovander MN, Serebryany SB. Tryptic fragments of the maleylated inclusion body protein of the silkworm nuclear polyhedrosis virus. II. Amino acid sequence of the fragments. Russian Journal of Bioorganic Chemistry. 1978; 4(8):1036-1047.
[9]
Katsman MS, Kozlov EA, Levitina TL, Gusak NM, Ovander MN, Serebryani SB. Peptides of partial acid and chymotryptic hydrolyses of polyhedral protein of nuclear polyhedrosis virus of Bombyx mori. Russian Journal of Bioorganic Chemistry. 1977; 3(11):1455-66
[10]
Levitina TL, Kozlov EA, SerebrianyÄ SB. Trypsin peptides of the polyhedral protein from the B. mori virus of nuclear polyhedrosis. Biokhimiia. 1976;41(2):228-36. Russian.
[11]
Easley CW. Combinations of specific color reactions useful in the peptide mapping technique. Biochim Biophys Acta. 1965;107(2):386-8.
[12]
Gusak NM, Ovander MN, Drobot LB, Serebryanyy SB. Determining the structure of peptides combined method dansyl-Edman. Molecular methods. biology. Kiev: Naukova Dumka. 1979:142-154.
[13]
Weiner AM, Platt T, Weber K. Amino-terminal sequence analysis of proteins purified on a nanomole scale by gel electrophoresis. J Biol Chem. 1972;247(10):3242-51.
[14]
Alakhov YuB, Bundule MA, Bundulis YuP, Vinokurov LM, Kozlov VP, Motuz LP. Primary structure of the elongation factor G from Escherichia coli. VI. Structure of peptides of cyanogen bromide cleavage of the G-factor molecule. Russian Journal of Bioorganic Chemistry. 1983; 9(3):304-14
[15]
Serebryani SB, Levitina TL, Kautsman ML, Radavski YL, Gusak NM, Ovander MN, et al. The primary structure of the polyhedral protein of nuclear polyhedrosis virus (NPV) of Bombyx mori. J Invert Pathol. 1977;30(3):442–3.
[16]
Kozlov EA, Levitina TL, Gusak NM, Ovander MN, Serebryany SB. Comparison of amino acid sequences of inclusion body proteins of nuclear polyhedrosis viruses of Bombyx mori, Porthetria dispar and Galleria mellonella. Russian Journal of Bioorganic Chemistry. 1981; 7(7):1008-1015.
[17]
Kozlov EA, Levitina TL, Gusak NM, Serebryany SB. Some physicochemical properties of the protein of inclusion bodies of the nuclear polyhedrosis and Granulosis viruses of Agrotis segetum. Biopolym. Cell. 1985; 1(3):121-4.
[18]
Kozlov EA, Levitina TL, Gusak NM. The primary structure of baculovirus inclusion body proteins. Evolution and structure-function aspects. Curr Top Microbiol Immunol. 1986;131:135-64.