Biopolym. Cell. 1989; 5(6):61-68.
Structure and Function of Biopolymers
Investigation of tryptic fragments of maleylated granulin of the Agrotis segetum granulosis virus
- Institute of Molecular Biology and Genetics, Academy of Sciences of the Ukrainian SSR
Kiev, USSR
Abstract
The granulin of the A. segetum granulosis virus was maleylated and subjected to tryptic digestion. The fragments were separated by gel filtration, ion-exchange chromalognaphy, butanol extraction and high-voltage paper electrophoresis and chromatography. Partial and complete ainino acid sequence of the 23 fragments including 293 amino acid residues was determined. 12 unique fragments comprise 222 residues and account for 90 % of the granulin polypeptide chain.
Full text: (PDF, in Russian)
References
[1]
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.
[2]
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.
[3]
Levitina TL, Rodnin NV, Gusak NM, Atepalikhina SA, Kozlov EA. Additional investigation of tryptic and chymotryptic peptides of the Agrotis segetum granulosis virus granulin. Biopolym. Cell. 1989; 5(6):52-60.
[4]
Kavsan VM, Katsman MS, Serebrianii SB. Extraction of polyhedral protein from Borrelinavirus bombycis by treating polyhedrons with acetic acid. Mikrobiol Zh. 1970;32(3):355-9.
[5]
Hirs CHW. Determination of cystine as cysteic acid. Methods Enzymol. 1967;59–62.
[6]
Kozlov EA, Levitina TL, Katsman MS, Serebryany SB. TryPtic fragments of the maleylated inclusion body protein of the silkworm nuclear polyhedrosis virus. I. Isolation and amino acid comPosition of the fragments. Russian Journal of Bioorganic Chemistry. 1978; 4 (8):1029-35.
[7]
Gray WR. Sequential degradation plus dansylation. Methods Enzymol. 1967;469–75.
[8]
Vinogradova EI, Feigina MIu, Aldanova NA, Lipkin VM. The primary structure of cytoplasmic aspartate aminotransferase from swine cardiac muscle. The amino acid sequence of soluble peptides of tryptic hydrolysis. Biokhimiia. 1973;38(1):3-21.
[9]
Reshetov PD, Chestukhina GG, Makhmutov S., Pyshkina AS. Thin layer Polyamide chromatograPhy. Khim Prir soedin. 1971; 1:66-88.
[10]
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.