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- W1987456323 abstract "A protein toxin, highly paralytic to insects, was purified from the venom of the scorpion Androctonus mauretanicus mauretanicus using permeation and ion exchange chromatography and the fly larvae contraction-paralysis bioassay. The purified toxin is about 330 times more toxic than the crude venom and is composed of 67 amino acids with an estimated mol. wt of 8129. The purified toxin binds selectively to homogenates of locust CNS in contrast to those from non-innervated locust tissues and crustacean CNS. Like A. a. Hector venom, the crude venom of A. m. mauretanicus also possesses a toxin(s) specifically affecting crustaceans. The present insect toxin, strongly resembles the toxin purified from the venom of the scorpion A. a. Hector in terms of its amino acid composition, molecular weight and selective binding affinity to insect nervous tissue. The apparent consistency in the chemical composition of the two insect toxins seems to be closely associated to their unique and highly selective mode of action." @default.
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- W1987456323 date "1979-01-01" @default.
- W1987456323 modified "2023-10-07" @default.
- W1987456323 title "The insect toxin from the venom of the scorpion Androctonus mauretanicus mauretanicus: Purification, characterization and specificity" @default.
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- W1987456323 doi "https://doi.org/10.1016/0020-1790(79)90081-7" @default.
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