Purification and characterization of a membrane-associated 48-kilodalton phospholipase A(2) in leaves of broad bean
- Authors
- Jung, KM; Kim, DK
- Issue Date
- Jul-2000
- Publisher
- AMER SOC PLANT PHYSIOLOGISTS
- Citation
- PLANT PHYSIOLOGY, v.123, no.3, pp 1057 - 1067
- Pages
- 11
- Journal Title
- PLANT PHYSIOLOGY
- Volume
- 123
- Number
- 3
- Start Page
- 1057
- End Page
- 1067
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/25307
- DOI
- 10.1104/pp.123.3.1057
- ISSN
- 0032-0889
1532-2548
- Abstract
- Se veral lines of evidence indicate that phospholipase A(2) (PLA(2)) plays a crucial role in plant cellular responses through production of linolenic acid, the precursor of jasmonic acid, from membrane phospholipids. Here we report the purification and characterization of a 48-kD PLA(2) from the membrane fractions of leaves of broad bean (Vicia faba). The plant PLA(2) was purified to near homogeneity by sequential column chromatographies from the membrane extracts. The purified 48-kD protein migrated as a single band on a SDS-PAGE gel and its density correlated with the PLA(2) activity. It was further confirmed that this 48-kD protein is the PLA(2) enzyme based on immunoprecipitating the activity with a monoclonal antibody against it and purifying the enzyme to homogeneity with the antibody affinity column. The purified plant PLA(2) preferred 2 linolenayl-sn-glycerol-3-phosphocholine (GPC) to 2-linoleoyl-GPC, 2-palmitoyl-GPC and 2-arachidonyl-GPC as substrates with a pH optimum at pH 7.0 to 8.0. The plant PLA(2) was activated by calmodulin and inhibited by pretreatment of 5,8,11,14-eicosatetraynoic acid known as an inhibitor of mammalian PLA(2)s. The enzyme was characterized as a Ca2+-independent PLA(2) different from mammalian PLA(2)s. This membrane-associated and Ca2+-independent PLA(2) is suggested to play an important role in the release of linolenic acid, the precursor of jasmonic acid, through a signal transduction pathway.
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