Role of the N-terminal region of the a chain in β1-bungarotoxin from the venom ofBungarus multicinctus (Taiwan-banded krait) View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1988-12

AUTHORS

L. S. Chang, C. C. Yang

ABSTRACT

The N-terminal α-amino groups of β1-bungarotoxin (β1-Bgt) fromBungarus multicinctus venom were modified with trinitrobenzene sulfonic acid and the modified derivative was separated by high performance liquid chromatography. The trinitrophenylated (TNP) derivative contained two TNP groups at the α-amino groups of A chain and B chain and showed a marked decrease in enzymatic activity. Methionine residues at positions 6 and 8 of the A chain were oxidized with chloramine T or cleaved with cyanogen bromide to remove the N-terminal octapeptide. Oxidation of methionine residues and removal of the N-terminal octapeptide caused a precipitous decrease in enzymatic activity, whereas antigenicity remained unchanged. The presence of dihexanoyllecithin influenced the interaction between β1-Bgt and 8-antilinonaphthalene sulfonate (ANS) and revealed that β1-Bgt consists of two types of ANS-binding sites, one at the substrate binding site of the A chain and the other might be at the B chain. The modified derivatives still retained their affinity for Ca2+ and ANS, indicating that the N-terminal region is not involved in Ca2+ and substrate binding. A fluorescence study revealed that the α-amino group of the A chain was in the vicinity of substrate binding site and that the TNP α-amino groups were in proximity to Trp-19 of the A chain. In addition, the study showed that the N-terminal region is important for stabilizing the architectural environment of Trp-19. The results, together with the proposal that Trp-19 of the A chain is involved in substrate binding, suggest that the N-terminal region of the A chain plays a crucial role in maintaining a functional active site for β1-Bgt. More... »

PAGES

713-727

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf01025579

DOI

http://dx.doi.org/10.1007/bf01025579

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1002907386

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/3252894


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