Abstract |
1. The lethal factor of the stonefish (Synanceja horrida) venom, designated as the stonustoxin, was purified to homogeneity by a two-step procedure on Sephacryl S-200 High Resolution (HR) gel permeation and DEAE Bio-Gel A anion exchange chromatography. 2. Stonustoxin has a native mol. wt of 148,000 and an isoelectric point of 6.9. 3. SDS- polyacrylamide gel electrophoresis revealed two subunits (designated alpha and beta) with mol. wts of 71,000 and 79,000, respectively. 4. The amino acid composition of both subunits and the N-terminal amino acid sequence of the beta subunit were also determined. 5. Purified stonustoxin had an LD50 of 0.017 microgram/g which is 22-fold more potent than that of the crude venom. 6. The toxin exhibited potent haemolytic activity in vitro and edema-inducing activity with a minimum edema dose (MED) of 0.15 micrograms in mouse paw. The edema effect was not antagonized by diphenhydramine.
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Authors | C H Poh, R Yuen, H E Khoo, M Chung, M Gwee, P Gopalakrishnakone |
Journal | Comparative biochemistry and physiology. B, Comparative biochemistry
(Comp Biochem Physiol B)
Vol. 99
Issue 4
Pg. 793-8
( 1991)
ISSN: 0305-0491 [Print] England |
PMID | 1790672
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Chemical References |
- Amino Acids
- Fish Venoms
- stonustoxin
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Topics |
- Amino Acid Sequence
- Amino Acids
(analysis)
- Animals
- Chromatography, High Pressure Liquid
- Chromatography, Ion Exchange
- Electrophoresis, Polyacrylamide Gel
- Fish Venoms
(chemistry, isolation & purification, toxicity)
- Fishes
- Isoelectric Point
- Male
- Mice
- Molecular Sequence Data
- Molecular Weight
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