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Hornetin: the lethal protein of the hornet ( Vespa flavitarsus ) venom
Author(s) -
Ho Chewn-Lang,
Ko Jane-Ling
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)81076-6
Subject(s) - venom , molecular mass , toxin , cysteine , biochemistry , gel permeation chromatography , amino acid , chemistry , biology , lysine , microbiology and biotechnology , organic chemistry , enzyme , polymer
By gel permeation on a Fractogel TSK HW 50 column followed by ion‐exchange chromatography on carboxymethylcellulose CM 52, a lethal protein, designated hornetin, was purified from the venom of Vespa flavitarsus . Hornetin is a highly basic protein (p I 10.2) with a molecular mass of about 32 kDa. Its amino acid composition is characterized by a high content of lysine, aspartic and glutamic acid, and is devoid of tryptophan and cysteine. The lack of cysteine in the molecule is distinct from other known vespid venom proteins of comparable size. The i.v. LD 50 of the toxin is 0.42 μg per g mouse. Assayed on the red blood cells of the mouse and guinea‐pig as well as isolated nerve muscle preparations of the chick and mouse, hornetin showed direct hemolytic activity and presynaptic neurotoxicity at microgram level and displayed musculotropic effect at higher concentrations.