On the purification of notexin: isolation of a single amino acid variant from the venom of Notechis scutatus scutatus

S. Chwetzoff, P. Mollier, F. Bouet, E.G. Rowan, A.L. Harvey, A. Menez

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

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 A2, 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 Ns, was an isofonn of notexin. Notechis Ns 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 Ns and notexin differed from each other by a single substitution amongst 119 amino acids: Lys → Arg at position 16.
Original languageEnglish
Pages (from-to)226-230
Number of pages4
JournalFEBS Letters
Volume261
Issue number2
DOIs
Publication statusPublished - 26 Feb 1990

Fingerprint

Purification
Amino Acids
Snakes
Poisons
Phospholipases A2
Ion Exchange Chromatography
Venoms
High performance liquid chromatography
Reverse-Phase Chromatography
Esterases
Chromatography
Staphylococcus aureus
Amino Acid Sequence
Ion exchange
Substitution reactions
High Pressure Liquid Chromatography
Notechis 11'2
notexin
Peptides
Chemical analysis

Keywords

  • notexin
  • isoform
  • phospholipase A2
  • reverse-phase high-performance liquid chromatography

Cite this

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title = "On the purification of notexin: isolation of a single amino acid variant from the venom of Notechis scutatus scutatus",
abstract = "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 A2, 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 Ns, was an isofonn of notexin. Notechis Ns 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 Ns and notexin differed from each other by a single substitution amongst 119 amino acids: Lys → Arg at position 16.",
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author = "S. Chwetzoff and P. Mollier and F. Bouet and E.G. Rowan and A.L. Harvey and A. Menez",
year = "1990",
month = "2",
day = "26",
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On the purification of notexin: isolation of a single amino acid variant from the venom of Notechis scutatus scutatus. / Chwetzoff, S.; Mollier, P.; Bouet, F.; Rowan, E.G.; Harvey, A.L.; Menez, A.

In: FEBS Letters, Vol. 261, No. 2, 26.02.1990, p. 226-230.

Research output: Contribution to journalArticle

TY - JOUR

T1 - On the purification of notexin: isolation of a single amino acid variant from the venom of Notechis scutatus scutatus

AU - Chwetzoff, S.

AU - Mollier, P.

AU - Bouet, F.

AU - Rowan, E.G.

AU - Harvey, A.L.

AU - Menez, A.

PY - 1990/2/26

Y1 - 1990/2/26

N2 - 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 A2, 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 Ns, was an isofonn of notexin. Notechis Ns 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 Ns and notexin differed from each other by a single substitution amongst 119 amino acids: Lys → Arg at position 16.

AB - 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 A2, 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 Ns, was an isofonn of notexin. Notechis Ns 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 Ns and notexin differed from each other by a single substitution amongst 119 amino acids: Lys → Arg at position 16.

KW - notexin

KW - isoform

KW - phospholipase A2

KW - reverse-phase high-performance liquid chromatography

UR - http://dx.doi.org/10.1016/0014-5793(90)80559-2

U2 - 10.1016/0014-5793(90)80559-2

DO - 10.1016/0014-5793(90)80559-2

M3 - Article

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JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 2

ER -