Biopolym. Cell. 1993; 9(4):44-49.
http://dx.doi.org/10.7124/bc.000365
Structure and Function of Biopolymers
Accelerated method of determination of the high-homologous proteins primary structures. Complete amino acid sequence of Mamestra brassicae nuclear polyhedrosis virus (NPV) polyhedrin
1Palchikovskaya L. I., 1Levitina T. L., 1Bobrovskaya M. T., 1Ovander M. N., 1Katsman M. S., 1Kozlov E. A.
  1. Institute of Molecular Biology and Genetics, NAS of Ukraine
    150, Akademika Zabolotnoho Str., Kyiv, Ukraine, 03680

Abstract

The accelerated method of amino acid sequence determination has been devised ("preparative finger print method"). The primary structure of the Mamestra brassicae nuclear polyhedrosis virus polyhedrin has been determined by this method. The complete amino acid sequence comparised 246 residues.
Full text: (PDF, in Russian)

References

[1] Kozlov EA, Levittna TL, Gusak NM, Rodnin NV, Atepalikhina SA, Palchykovska LH. 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. Biopolym Cell. 1991; 7(1):75-82.
[2] Kozlov EA, Rodnin NV, Levitina TL, Gusak NM, Atepalikhina SA. Primary structure of granulin of the granulosis virus of Agrotis segetum. Bioorg Khim. 1990;16(12):1675-7.
[3] Rohrmann GF. Polyhedrin structure. J Gen Virol. 1986;67 ( Pt 8):1499-513.
[4] Cameron IR, Possee RD. Conservation of polyhedrin gene promoter function between Autographa californica and Mamestra brassicae nuclear polyhedrosis viruses. Virus Res. 1989;12(3):183-99.
[5] Oakey R, Cameron IR, Davis B, Davis E, Possee RD. Analysis of transcription initiation in the Panolis flammea nuclear polyhedrosis virus polyhedrin gene. J Gen Virol. 1989;70 ( Pt 3):769-75.
[6] Akiyoshi D, Chakerian R, Rohrmann GF, Nesson MH, Beaudreau GS. Cloning and sequencing of the granulin gene from the Trichoplusia ni granulosis virus. Virology. 1985;141(2):328-32.
[7] Chakerian R, Rohrmann GF, Nesson MH, Leisy DJ, Beaudreau GS. The nucleotide sequence of the Pieris brassicae granulosis virus granulin gene. J Gen Virol. 1985;66 ( Pt 6):1263-9.
[8] 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.
[9] Kozlov EA, Serebryany SB. Structure of certain tryptic peptides of the polyhedrin of the Mamestra brassicae nuclear polyhedrosis virus. Biopolym Cell. 1985; 1(4):194-8.
[10] Cleland WW. Dithiothreitol, A new protective reagent for sh groups. Biochemistry. 1964;3:480-2.
[11] Kozlov E. A., Levitina T. L., Katsman M. S., Gusak N. M., Ovander M. N., Serebryany S. B. 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.
[12] Kavsan VM, Moroz LV, Serebrianyi SB. Simplified instrument for horizontal high-voltage paper electrophoresis. Ukr Biokhim Zh. 1968;40(1):104-7.
[13] Gusak NM, Ovander MN, Drobot LB, Serebryanyy SB. Determining the structure of peptides combined method Dansyl-Edman. Molecular methods. biology. Kiev, Naukova Dumka, 1979; 142-54.
[14] Easley CW. Combinations of specific color reactions useful in the peptide mapping technique. Biochim Biophys Acta. 1965;107(2):386-8.
[15] Kozlov EA, Levitina TL, Gusak NM, Larionov GV, VeremeД­chenko SN. Comparative biochemical studies of polyhedral proteins of nuclear polyhedrosis viruses. Biokhimiia. 1978;43(12):2189-95.
[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):1008-15.