Limited proteolysis of Bacillus thuringiensis CryIG and CryIVB δ- endotoxins leads to formation of active fragments that do not coincide with the structural domains

Journal of Protein Chemistry

Volumn 17, Issue 5, 1998, Pages 463-471

  Zalunin, Igor A ^a   Revina, Lyudmila P ^a   Kostina, Lyubov I ^a   Chestukhina, Galina G ^a   Stepanov, Valentin M ^a  

^a STATE RESEARCH INSTITUTE OF GENETICS AND SELECTION OF INDUSTRIAL MICROORGANISMS   (Russian Federation)

Author keywords

endotoxin; Bacillus thuringiensis; Domains; Limited proteolysis

Indexed keywords

ENDOTOXIN;

AMINO ACID SEQUENCE; ARTICLE; BACILLUS THURINGIENSIS; NONHUMAN; PEPTIDE ANALYSIS; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN DEGRADATION; STRUCTURE ANALYSIS; TOXIN ANALYSIS;

AEDES; AMINO ACID SEQUENCE; ANIMALS; BACTERIAL PROTEINS; BACTERIAL TOXINS; ENDOTOXINS; HEMOLYSIN PROTEINS; HYDROLYSIS; LARVA; MANDUCA; MOLECULAR SEQUENCE DATA; PEST CONTROL, BIOLOGICAL; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 0031826689     PISSN: 02778033     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1022522602400     Document Type: Article

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