Open AccessAmino‐Acid Sequence of the α‐Subunit of Taipoxin, an Extremely Potent Presynaptic Neurotoxin from the Australian Snake Taipan ( Oxyurunus s. scutellatus )
Author(s) -
LIND Peter,
EAKER David
Publication year - 1982
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1982.tb06612.x
Subject(s) - edman degradation , venom , neurotoxin , peptide sequence , protease , amino acid , biochemistry , biology , serine protease , snake venom , microbiology and biotechnology , enzyme , chemistry , gene
The amino acid sequence of the α‐subunit of taipoxin, an extremely potent presynaptic neurotoxin from the Australian snake taipan has been determined. The very basic protein, by itself a moderately neurotoxic phospholipase, consists of a single polypeptide chain of 119 amino acids. The main fragmentation of the reduced and S‐carboxymethylated derivative was accomplished by cleavage with Staphylocoeus aureus V8 pro‐ tease and trypsin. Chymotryptic peptides and cyanogen bromide fragments were used to align and complete the sequence, which was determined by automated Edman degradation. The taipoxin γ‐subunit is closely homologous to the other taipoxin subunits and to other elapid snake venom phospholipases A 2 .