Additional investigation of tryptic and chymotryptic peptides of the Agrotis segetum granulosis virus granulin

Authors

  • T. L. Levitina Institute of Molecular Biology and Genetics, Academy of Sciences of the Ukrainian SSR Kiev, USSR Author
  • N. V. Rodnin Institute of Molecular Biology and Genetics, Academy of Sciences of the Ukrainian SSR Kiev, USSR Author
  • N. M. Gusak Institute of Molecular Biology and Genetics, Academy of Sciences of the Ukrainian SSR Kiev, USSR Author
  • S. A. Atepalikhina Institute of Molecular Biology and Genetics, Academy of Sciences of the Ukrainian SSR Kiev, USSR Author
  • E. A. Kozlov Institute of Molecular Biology and Genetics, Academy of Sciences of the Ukrainian SSR Kiev, USSR Author

DOI:

https://doi.org/10.7124/bc.0000F7

Abstract

20 tryptic and 81 chymotryptic peptides were isolated and their partial or complete amino acid sequence was determined.

References

Levitina TL, Serebryany SB, Rodnin NV, Kozlov EA. The structure of some tryptic peptides of the Agrotis segetum granulosis virus granulin. Biopolym. Cell. 1986; 2(1):30-5.

Levitina TL, Rodnin NV, Serebryany SB, Kozlov EA. The structure of certain chymotryptic peptides of the Agrotis segetum granulosis virus granulin. Biopolym. Cell. 1986; 2(2):73-81.

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.

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.

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.

Published

1989-11-20

Issue

Section

Structure and Function of Biopolymers