Purification and properties of three new phospholipase A(2) isoenzymes from Micropechis ikaheka venom

Citation
R. Gao et al., Purification and properties of three new phospholipase A(2) isoenzymes from Micropechis ikaheka venom, BBA-PROT ST, 1545(1-2), 2001, pp. 30-40
Citations number
48
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY
ISSN journal
0167-4838 → ACNP
Volume
1545
Issue
1-2
Year of publication
2001
Pages
30 - 40
Database
ISI
SICI code
0167-4838(20010209)1545:1-2<30:PAPOTN>2.0.ZU;2-W
Abstract
Three new phospholipase Al (PLA(2)) isoenzymes were purified from the Micro pechis ikaheka venom by successive chromatographies. The homogeneity of the m was accessed by capillary zone electrophoresis and mass spectrometry. The ir N-terminal sequences showed high identity (94, 88 and 90, respectively) with MiPLA-1, a group IB PLA(2) also from this venom. In addition, strong i mmuno-cross-reaction with anti-MiPLA-1 serum was observed. These results su ggested that three newly purified PLA(2)! belonged to group IB. Beside enzy matic activity, they induced various pharmacological effects, including myo toxic, anticoagulant effects and insulin secretion stimulating effects. Our results indicated that enzymatic activity is essential for their myotoxic and anticoagulant effects. On the other hand, no direct correlation between their insulin secretion stimulating effect and enzymatic activity was obse rved, suggesting that they may stimulate insulin secretion through a nonenz ymatic mechanism. (C) 2001 Elsevier Science B.V. All rights reserved.