Purification and properties of phospholipase A2 from the venom of scorpion, (Heterometrus fulvipes)
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- PMID: 2112384
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Purification and properties of phospholipase A2 from the venom of scorpion, (Heterometrus fulvipes)
Biochem Int.
1990.
Abstract
Phospholipase A2 was purified about 78 fold from the venom of scorpion Heterometrus fulvipes. The molecular weight of the enzyme was found to be 16,000 and it was optimally active at pH 7.4 and at 50 degrees C. The Km value of the enzyme was 1.8 x 10(-3) M. Calcium, Magnesium and Zinc ions stimulated whereas Mercury ion and EDTA inhibited the enzyme activity. This enzyme exhibited fluorescence emission maximum between 310-320 nm.
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