Phospholipase A from Bee Venom

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Crystal structure of bee-venom phospholipase A2: correction.

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Inhibition of beta-bungarotoxin action by bee venom phospholipase A2.

(3-Bungarotoxin ((3-BuTX) induces twitching of innervated frog muscle and subsequently blocks transm itter release from motor nerve endings. These actions of P-BuTX are prevented if the nerve-muscle junctions are pretreated with a low concentration of phospholipase A2 from bee venom. When the Ca2+ in the external fluid is replaced by Sr2+, the phospho­ lipase activity of P-BuTX is negligible an...

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Bee Venom Phospholipase A2: Yesterday’s Enemy Becomes Today’s Friend

Bee venom therapy has been used to treat immune-related diseases such as arthritis for a long time. Recently, it has revealed that group III secretory phospholipase A2 from bee venom (bee venom group III sPLA2) has in vitro and in vivo immunomodulatory effects. A growing number of reports have demonstrated the therapeutic effects of bee venom group III sPLA2. Notably, new experimental data have...

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Crystal structure of bee-venom phospholipase A2 in a complex with a transition-state analogue.

The 2.0 angstroms crystal structure of a complex containing bee-venom phospholipase A2 (PLA2) and a phosphonate transition-state analogue was solved by multiple isomorphous replacement. The electron-density map is sufficiently detailed to visualize the proximal sugars of the enzyme's N-linked carbohydrate and a single molecule of the transition-state analogue bound ot its active center. Althoug...

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ژورنال

عنوان ژورنال: European Journal of Biochemistry

سال: 1971

ISSN: 0014-2956,1432-1033

DOI: 10.1111/j.1432-1033.1971.tb01414.x