Characterization of a membrane-associated apoplastic lipoxygenase in Phaseolus vulgaris L |
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Authors: | Sicilia Francesca Mattei Benedetta Cervone Felice Bellincampi Daniela De Lorenzo Giulia |
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Affiliation: | Dipartimento di Biologia Vegetale, Università di Roma La Sapienza, Piazzale Aldo Moro 5, Roma 00185, Italy. |
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Abstract: | An extracytoplasmic 86.7 kDa protein was isolated from intercellular washing fluids (IWF) of Phaseolus vulgaris etiolated hypocotyls. Micro sequencing of tryptic peptides of the 86.7 kDa protein revealed 100% identity with a bean lipoxygenase (LOX) protein fragment. Purified P87-LOX exhibited LOX activity characterized by an optimal pH of 6.0 and linolenic acid as an optimal substrate, and was classified as a 13-LOX with respect to its positional specificity of linoleic acid oxygenation. A protein identical to P87-LOX, as determined by MALDI-TOF analysis and biochemical characterization, was purified from hypocotyl microsomes. Immunoblot analysis showed that P87-LOX is present in plasma membrane-enriched fractions, from which it was solubilized using high ionic strength buffers. These observations suggest that P87-LOX is a peripheral protein associated to the apoplastic face of the plasma membrane. |
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