Characterization and Gene Organization of Taiwan Banded Krait (Bungarus multicinctus) γ-Bungarotoxin View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2002-05

AUTHORS

Long-Sen Chang, Charling Chung, Bin-Nan Wu, Chen-Chung Yang

ABSTRACT

γ-Bungarotoxin was isolated from Bungarus multicinctus (Taiwan banded krait) venom using a combination of chromatography on a SP-Sephadex C-25 column and a reverse-phase high-performance liquid chromatography column. Circular dichroism (CD) measurement revealed that its secondary structure was dominant with β-sheet structure as is that of snake venom α-neurotoxins and cardiotoxins. γ-Bungarotoxin exhibits activity on inhibiting the binding of [3H]quinuclidinyl benzilate to the M2 muscarinic acetylcholine receptor subtype, and competes weakly with radioiodinated α-bungarotoxin for binding to the Torpedo nicotinic acetylcholine receptor. Moreover, the toxin inhibits collagen-induced platelet aggregation, with an IC50 of approximately 200 nM. The genomic DNA encoding the γ-bungarotoxin precursor is amplified by polymerase chain reaction (PCR). The gene is organized with three exons separated by two introns, and shares virtually identical overall organization with those reported for α-neurotoxin and cardiotoxin genes, including similar intron insertions. The intron sequences of these genes share sequence identity up to 85%, but the exon sequences are highly variable. These observations suggest that γ-bungarotoxin, α-neurotoxins, and cardiotoxins originate from a common ancestor, and the evolution of these genes shows a tendency to diversify the functions of snake venom proteins. More... »

PAGES

223-229

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1023/a:1019760401692

DOI

http://dx.doi.org/10.1023/a:1019760401692

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1014509207

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/12168693


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