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On the purification of notexin
Author(s) -
Chwetzoff Serge,
Mollier Pascale,
Bouet Françoise,
Rowan Edward G.,
Harvey Alan L.,
Ménez André
Publication year - 1990
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(90)80559-2
Subject(s) - biochemistry , in vitro , venom , protease , amino acid , chemistry , pyroglutamic acid , peptide sequence , phospholipase , biology , enzyme , gene
Venom of the Australian tiger snake, Notechis scutatus scutatus was fractionated by conventional ion‐exchange chromatography. The fraction containing notexin, a well‐known single‐chain toxic phospholipase A 2 , was further purified by reverse‐phase high‐performance liquid chromatography. Two main components were isolated and the major one corresponded to notexin. The other component, designated as notechis N s , was an isofonn of notexin. Notechis N s and notexin possessed similar in vitro esterase activity, in vitro neuromuscular activity and in vivo lethality. Amino acid composition and sequence of the Staphylococcus aureus V8‐protease peptides demonstrated that primary structures of notechis N s and notexin differed from each other by a single substitution amongst 119 amino acids: Lys → Arg at position 16.