Edema factor from the venom of Trimeresurus elegans (Sakishimahabu).

Abstract

An edema factor was isolated from the venom of Trimeresurus elegans using HW-55, CM-Cellulose, and Mono S column chromatographies. Homogeneity was demonstrated by the formation of a single band in polyacrylamide gel electrophoresis (pH 8.3). The edema factor has a molecular weight of 25,500, an isoelectric point of 7.5, and express edema, proteolytic and capillary permeability-increasing activities. Edema, proteolytic and capillary permeability-increasing activities are inhibited by ethylenediaminetetraacetic acid (EDTA), o-phenanthroline, and N-bromosuccinimide. Additionally, this factor exhibits kinin-releasing activity. The edema factor possesses proteolytic activity as shown by hydrolyzing the Val(3)-Asn(4), His(5)-Leu(6), Ser(9)-His(10), Ala(14)-Leu(15), Leu(15)-Tyr(16), Tyr(16)-Leu(17), and Glu(21)-Arg(22) bonds of oxidized insulin B chain. The A alpha, B beta, and gamma chains of human fibrinogen were also hydrolyzed. The edema factor was found to contain 1 mol of zinc and 2 mols of calcium per mol of protein and the amino-terminal sequence was determined.

• Authors: T Nikai, Y Suzuki, Y Komori, H Sugihara
• Journal: Journal of natural toxins (J Nat Toxins) Vol. 9 Issue 2 Pg. 147-58 (May 2000) ISSN: 1058-8108 [Print] United States
• PMID: 10868342 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Amino Acids
• Crotalid Venoms
• Trimeresurus venoms
• Viper Venoms
• edema factor
• Endopeptidases
• elegatoxin

Topics

• Amino Acid Sequence
• Amino Acids (analysis)
• Animals
• Crotalid Venoms (chemistry)
• Edema (chemically induced)
• Endopeptidases (chemistry)
• Humans
• Mice
• Molecular Sequence Data
• Molecular Weight
• Trimeresurus
• Viper Venoms (chemistry)