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- W2000233912 abstract "The importance of the invariant arginine-36 in cardiotoxin was investigated by chemical modification. Reaction of the single arginine residue in Naja haje annulifera venom cardiotoxin V111 with 1,2-cyclohexanedione yielded derivative 1 (cardiotoxin V111 modified at Arg-36). Purification was achieved using cation-exchange chromatography in the presence of borate ions. The reaction was reversible by incubation with hydroxylamine at 37°C. Derivative 1 had an intravenous LD50 of 17 μg·g−1 in mice, the borate complex of the derivative an LD50 of 14 gmg·g−1, and the maternal resulting from the reversal of the reaction, 5.9 μg·g−1, as compared to an LD50 of 4.5 μg·g−1 for the native toxin. Circular dichroism spectra in borate buffer (pH 8.0) and glycine-HCl (pH 3.5) showed that the derivative had not undergone severe conformational changes. Because some lethality was retained after making the derivative, it is doubtful whether Arg-36 can be considered to be of crucial importance for the biological action of cardiotoxin and it probably fulfils a structural role." @default.
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- W2000233912 date "1983-07-01" @default.
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- W2000233912 title "The modification of arginine-36 in elapid venom cardiotoxin using 1,2-cyclohexanedione" @default.
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- W2000233912 doi "https://doi.org/10.1016/0167-4838(83)90005-5" @default.
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