Lys-49 phospholipases A2 as active enzymes for beta-arachidonoyl phospholipid bilayer membranes
artículo original
Fecha
1997Autor
Yamaguchi, Yoko
Shimohigashi, Yasuyuki
Chiwata, Tsuyoshi
Tani, Ayako
Chijiwa, Takahisa
Lomonte, Bruno
Ohno, Motoroni
Metadatos
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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.
External link to the item
10.1080/15216549700203771Colecciones
- Microbiología [1170]