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We report here the construction of cardiotoxin V gene, from cobra snake venom (Naja naja atra), by chemically synthesized oligonucleotides and its expression as a glutathione S-transferase-cardiotoxin fusion protein in the inclusion bodies of Escherichia coli. The expression of cardiotoxin fusion protein in protein with a yield of about 35 mg/liter culture was confirmed by highly specific anti-peptide antibodies generated against the unique amino acid residues located at the tip of loop II of cardiotoxin V. Since the fusion protein can be easily treated by CNBr to free the toxin moiety, as revealed by immunoblotting of the cleaved protein, the results provide an avenue for future structural and functional studies of cardiotoxin molecules.
L M Chi, and
A A Vyas, and
G S Rule, and
W G Wu
March 1992,
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L M Chi, and
A A Vyas, and
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W G Wu
August 2004,
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L M Chi, and
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August 1996,
Proceedings of the National Academy of Sciences of the United States of America,
L M Chi, and
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G S Rule, and
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L M Chi, and
A A Vyas, and
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L M Chi, and
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L M Chi, and
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W G Wu
January 1995,
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L M Chi, and
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Protein expression and purification,
L M Chi, and
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W G Wu
March 2003,
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L M Chi, and
A A Vyas, and
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W G Wu
May 1990,
Archives of biochemistry and biophysics,
