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dc.creatorYamaguchi, Yoko
dc.creatorShimohigashi, Yasuyuki
dc.creatorChiwata, Tsuyoshi
dc.creatorTani, Ayako
dc.creatorChijiwa, Takahisa
dc.creatorLomonte, Bruno
dc.creatorOhno, Motoroni
dc.date.accessioned2017-09-28T15:31:31Z
dc.date.available2017-09-28T15:31:31Z
dc.date.issued1997
dc.identifier.citationhttp://onlinelibrary.wiley.com/doi/10.1080/15216549700203771/abstract
dc.identifier.issn1039-9712
dc.identifier.urihttps://hdl.handle.net/10669/73302
dc.description.abstractPhospholipases 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.es_ES
dc.language.isoen_USes_ES
dc.sourceBiochemistry and Molecular Biology International; Volumen 43, Número 1.1997es_ES
dc.subjectPhospholipases A2es_ES
dc.subjectLys-49-phospholipases A2es_ES
dc.subjectLipolytic activityes_ES
dc.subjectArachidonatees_ES
dc.titleLys-49 phospholipases A2 as active enzymes for beta-arachidonoyl phospholipid bilayer membraneses_ES
dc.typeartículo científico
dc.identifier.doi10.1080/15216549700203771
dc.description.procedenceUCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)es_ES
dc.identifier.pmid9315278


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