Lys-49 phospholipases A2 as active enzymes for beta-arachidonoyl phospholipid bilayer membranes
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| Autores: | , , , , , , |
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| Formato: | artículo original |
| Fecha de Publicación: | 1997 |
| Descripción: | Phospholipases A2 containing Lys-49 have been reported to be extremely weak or inactive as enzyme. We have recently shown that basic proteins I and II (BP-I and BP-II), Lys- 49-PLA2s isolated from the venom of Trimeresurus flavoviridis (Habu snake), are potent to hydrolyze the arachidonate of 2-arachidonoyl-l-stearoyl-L-3-phosphatidylcholine (ASPC) in bilayer vesicles. In order to ensure such enzymatic activity of Lys-49-PLA2s, two other Lys-49- PLA2s from different snake venoms, myotoxin II (from Bothrops asper) and App-K49 (form Agkistrodon piscivorus piscivorus), were examined. Myotoxin II was found to be very active, even more potent than BP-II, liberating about 80% of arachidonic acid from liposomes. App-K49 was also active (about 50%) for ASPC liposomes. They were very weak or almost inactive for ASPC micelles and monomers. All these Lys-49-PLA2s were inactive for ASPC liposomes in the absence of Ca 2+. These results clearly demonstrated that Lys-49-PLA2s are the enzymes to hydrolyze the C2-ester bond of ASPC in bilayer membranes. |
| País: | Kérwá |
| Institución: | Universidad de Costa Rica |
| Repositorio: | Kérwá |
| OAI Identifier: | oai:kerwa.ucr.ac.cr:10669/73302 |
| Acceso en línea: | http://onlinelibrary.wiley.com/doi/10.1080/15216549700203771/abstract https://hdl.handle.net/10669/73302 |
| Palabra clave: | Phospholipases A2 Lys-49-phospholipases A2 Lipolytic activity Arachidonate |