Detection of two phospholipase A2(PLA2) activities in leaves of higher plant Vicia faba and comparison with mammalian PLA2's

Dae Kyong Kim, Ho Joung Lee, Youngsook Lee

Research output: Contribution to journalArticlepeer-review

32 Citations (Scopus)


Leaves of higher plant Vicia faba contains two Phospholipase A2 (PLA2) activities which are detected in cytosolic fractions. Based on a gel filtration column chromatography, two cytosolic PLA2 activities migrated with molecular masses of 70 kDa and 14 kDa. The first (70 kDa peak) was optimally active at pH 4.5 and was not dependent on [Ca2+ for its activity. In the presence of 5 mM CaCl2, 'phospholipase B' activity was shown in the 70 kDa peak. The second (14 kDa peak) was optimally active in the pH range 9-10 and required millimolar concentrations of calcium for optimal activity. The two activities were not inhibited by dithiothreitol. Neither anti-pancreatic PLA2 antiserum nor anti-(pig spleen 100 kDa cytosolic PLA2) antiserum immunoprecipitated any activity of the two plant PLA2's. The present results indicate that at least the 14 kDa form of the two PLA2 enzymes detected in leaves of higher plants is biochemically and immunochemically different from the well characterized Ca2+-dependent mammalian PLA2's.

Original languageEnglish
Pages (from-to)213-218
Number of pages6
JournalFEBS Letters
Issue number3
Publication statusPublished - 1994 May 2
Externally publishedYes


  • Free fatty acid
  • Lysophospholipid
  • Plant phospholipase A
  • Vicia faba

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


Dive into the research topics of 'Detection of two phospholipase A<sub>2</sub>(PLA<sub>2</sub>) activities in leaves of higher plant Vicia faba and comparison with mammalian PLA<sub>2</sub>'s'. Together they form a unique fingerprint.

Cite this