Separation and characterization of the A chain and B chain in β1-bungarotoxin fromBungarus multicinctus (Taiwan banded krait) venom View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1993-08

AUTHORS

L. S. Chang, C. C. Yang

ABSTRACT

The interchain disulfide bond between A chain and B chain of β1-bungarotoxin (β1-Bgt) was selectively cleaved by dithiothreitol, and the A and B chains were separated by HPLC. The separated A and B chains did not show detectable enzymatic activity and lethal toxicity, but exhibited an immunoreactivity with anti-β1-Bgt antibody. Analytical isoelectrofocusing revealed that the A chain is a neutral subunit with pI=7.4, and the B chain is a basic one with pI=9.6. The A chain exhibited a Ca2+-binding ability as revealed by fluorescence measurement. Moreover, fluorescence studies showed that the intact interchain disulfide bond is essential for maintaining the hydrophobic character of substrate binding site in β1-Bgt and stabilizing the architectural environment of Trp-19 in the A chain. However, combination of the A chain and B chain failed to restore the biological activities and physicochemical properties which the intact β1-Bgt possessed. These, together with our previous result that the Trp-19 of the A chain is involved in substrate binding, suggest that the integrity of the interchain disulfide bond favors the maintenance of the active conformation of β1-Bgt. More... »

PAGES

469-475

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf01025047

DOI

http://dx.doi.org/10.1007/bf01025047

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1033026759

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/8251067


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