Isolation, purification and immunological evaluation of toxin Hb from scorpion Heterometrus bengalensis (C.L. Koch) venom.
Toxin-Hb, a lethal toxic antigenic protein, isolated from the venom of H. bengalensis by CM-cellulose ion-exchange chromatography was a heat labile basic protein with a molecular weight of 10 kDa. It produced irreversible blockade on the isolated rat phrenic nerve diaphragm and chick biventer cervicis. LD50 of toxin Hb was 0.48 mg/kg (iv) in mice. Antiserum was raised in mice by hyperimmunization against toxin Hb. Antitoxin Hb antiserum was immunologically potent as revealed by immunogel-diffusion and immunoelectrophoresis. Five fold protection against the lethal action of toxin Hb was achieved by the antiserum. It also effectively antagonised toxin Hb induced neuromuscular blockade on isolated rat phrenic nerve diaphragm and chick biventer cervicis preparations.
Dasgupta
S C
SC
Department of Pharmacology, School of Tropical Medicine, Calcutta, India.
Gomes
A
A
Gomes
A
A
Basu
A
A
Lahiri
S C
SC
D000818:Animals; D002645:Chickens; D002852:Chromatography, Ion Exchange; D007106:Immune Sera; D051379:Mice; D051381:Rats; D012604:Scorpion Venoms / Q000276:immunology / Q000302:isolation & purification* / Q000633:toxicity; D012605:Scorpions; D013696:Temperature
D007106:Immune Sera; D012604:Scorpion Venoms