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Purification and Characterization of a Low-Molecular-Weight Phospholipase A2 from Developing Seeds of Elm1

Ulf Ståhl*, Bo Ek, and Sten Stymne

Department of Plant Biology, P.O. Box 7080, Swedish University of Agricultural Sciences, S-750 07 Uppsala, Sweden (U.S., B.E.); and Department of Plant Breeding Research, Swedish University of Agricultural Sciences, Herman von Ehles v. 4-6, S-268 31 Svalöv, Sweden (S.S.)

Phospholipase A2 (PLA2) was purified about 180,000 times compared with the starting soluble-protein extract from developing elm (Ulmus glabra) seeds. On sodium dodecyl sulfate-polyacrylamide gel electrophoresis the purified fraction showed a single protein band with a mobility that corresponded to 15 kD, from which activity could be recovered. When analyzed by matrix-assisted laser-desorption ionization-time-of-flight mass spectrometry, the enzyme had a deduced mass of 13,900 D. A 53-amino acid-long N-terminal sequence was determined and aligned with other sequences, giving 62% identity to the deduced amino acid sequence of some rice (Oryza sativa) expressed sequence tag clones. The purified enzyme had an alkaline pH optimum and required Ca2+ for activity. It was unusually stable with regard to heat, acidity, and organic solvents but was sensitive to disulfide bond-reducing agents. The enzyme is a true PLA2, neither hydrolyzing the sn-1 position of phosphatidylcholine nor having any activity toward lysophosphatidylcholine or diacylglycerol. The biochemical data and amino acid sequence alignments indicate that the enzyme is related to the well-characterized family of animal secretory PLA2s and, to our knowledge, is the first plant enzyme of this type to be described.

1   This research was supported by the Swedish Agricultural and Forestry Research Council, the Swedish Foundation for Strategic Research, the Swedish Farmers Research Foundation, and Metapontum Agrobios (Metaponto, Italy).
*   Corresponding author; e-mail ulf.stahl{at}vbiol.slu.se; fax 46-18-673279.

Plant Physiol. (1998) 117: 197-205
Copyright Clearance Center:   0032-0889/98/117/0197/09
© 1998 American Society of Plant Physiologists




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