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Primary structure of α‐bungarotoxin Six amino acid residues differ from the previously reported sequence
Author(s) -
Ohta Mitsuhiro,
Ohta Kiyoe,
Nishitani Hiroshi,
Hayashi Kyozo
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80195-3
Subject(s) - bungarotoxin , protein primary structure , primary (astronomy) , sequence (biology) , chemistry , peptide sequence , amino acid residue , stereochemistry , biochemistry , acetylcholine receptor , physics , receptor , gene , astronomy
α‐Bungarotoxin (α‐BuTx) was isolated from the venom of the Formosan banded krait ( Bungarus multicinctus ). The amino acid sequence was determined by a combination of conventional methods. In contrast to the sequence of α‐BuTx reported by Mebs et al. [(1971) Biochem. Biophys. Res. Commun. 44, 711–716], our results revealed the presence of ‐Pro‐ , ‐ and ‐ at positions 9–11, 67–68 and 71–72 from the amino‐terminal, respectively, and not ‐Pro‐ , ‐ and ‐ as reported previously.