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Two novel proteins, BM8 and BM14, were isolated fromBungarus multicinctus (Taiwan banded krait) venom using the combination ofchromatography on a SPSephadex C-25 column and a reversephase HPLC column. Bothproteins contained 82 amino acid residues including 10 cysteine residues, butthere were two amino acid substitutions at positions 37 and 38 (Glu37Ala38 inBM8; Lys37Lys38 in BM14). CD spectra and acrylamide quenching studies revealedthat the gross conformation of BM8 and BM14 differed. In contrast to BM8, BM14inhibited the binding of [3H]quinuclidinyl benzilate to the M2 muscarinicacetylcholine (mAchR) receptor subtype. Trinitrophenylation of Lys residuesabolished the mAchRbinding activity of BM14, indicating that the Lyssubstitutions at positions 37 and 38 played a crucial role in the activity ofBM14. The genomic DNA encoding the precursor of BM14 was amplified by PCR. Thegene shared virtually identical structural organization with αneurotoxin andcardiotoxin genes. The intron sequences of these genes shared a sequenceidentity up to 84%, but the proteincoding regions were highly variable. Theseresults suggest that BM8, BM14, neurotoxins and cardiotoxins may haveoriginated from a common ancestor, and the evolution of snake venom proteinsshows a tendency to diversify their functions.

Muscarinic Toxin-Like Proteins from Taiwan Banded Krait (Bungarus multicinctus) Venom: Purification, Characterization and Gene Organization