Abstract
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 language | English |
|---|---|
| Pages (from-to) | 213-218 |
| Number of pages | 6 |
| Journal | FEBS Letters |
| Volume | 343 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - 1994 May 2 |
| Externally published | Yes |
Fingerprint
Keywords
- Free fatty acid
- Lysophospholipid
- Plant phospholipase A
- Vicia faba
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
Detection of two phospholipase A2(PLA2) activities in leaves of higher plant Vicia faba and comparison with mammalian PLA2's. / Kyong Kim, Dae; Lee, Hojoung; Lee, Youngsook.
In: FEBS Letters, Vol. 343, No. 3, 02.05.1994, p. 213-218.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Detection of two phospholipase A2(PLA2) activities in leaves of higher plant Vicia faba and comparison with mammalian PLA2's
AU - Kyong Kim, Dae
AU - Lee, Hojoung
AU - Lee, Youngsook
PY - 1994/5/2
Y1 - 1994/5/2
N2 - 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.
AB - 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.
KW - Free fatty acid
KW - Lysophospholipid
KW - Plant phospholipase A
KW - Vicia faba
UR - http://www.scopus.com/inward/record.url?scp=0028181660&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0028181660&partnerID=8YFLogxK
U2 - 10.1016/0014-5793(94)80558-X
DO - 10.1016/0014-5793(94)80558-X
M3 - Article
C2 - 8174704
AN - SCOPUS:0028181660
VL - 343
SP - 213
EP - 218
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 3
ER -