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|Title:||Purification and properties of three new phospholipase A2isoenzymes from Micropechis ikaheka venom|
|Keywords:||Amino acid sequence|
|Source:||Gao, R., Selvanayagam, Z.E., Gopalakrishnakone, P., Kini, R.Manjunatha, Li, G., Luo, R. (2001). Purification and properties of three new phospholipase A2isoenzymes from Micropechis ikaheka venom. Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology 1545 (1-2) : 30-40. ScholarBank@NUS Repository. https://doi.org/10.1016/S0167-4838(00)00258-2|
|Abstract:||Three new phospholipase A2 (PLA2) isoenzymes were purified from the Micropechis ikaheka venom by successive chromatographies. The homogeneity of them was accessed by capillary zone electrophoresis and mass spectrometry. Their N-terminal sequences showed high identity (94, 88 and 90, respectively) with MiPLA-1, a group IB PLA2 also from this venom. In addition, strong immuno-cross-reaction with anti-MiPLA-1 serum was observed. These results suggested that three newly purified PLA2 belonged to group IB. Beside enzymatic activity, they induced various pharmacological effects, including myotoxic, 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 observed, suggesting that they may stimulate insulin secretion through a non-enzymatic mechanism. © 2001 Elsevier Science B.V.|
|Source Title:||Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology|
|Appears in Collections:||Staff Publications|
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