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

Dae Kyong Kim, Hojoung Lee, Youngsook Lee

Research output: Contribution to journalArticle

30 Citations (Scopus)

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 languageEnglish
Pages (from-to)213-218
Number of pages6
JournalFEBS Letters
Volume343
Issue number3
DOIs
Publication statusPublished - 1994 May 2
Externally publishedYes

Fingerprint

Vicia faba
Plant Leaves
Phospholipases A2
Cytosolic Phospholipases A2
Immune Sera
Lysophospholipase
Column chromatography
Dithiothreitol
Molecular mass
Gel Chromatography
Swine
Spleen
Gels
Calcium
Enzymes

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 journalArticle

@article{db87cba35a0246a3ab8f13c0f8c6cd24,
title = "Detection of two phospholipase A2(PLA2) activities in leaves of higher plant Vicia faba and comparison with mammalian PLA2's",
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.",
keywords = "Free fatty acid, Lysophospholipid, Plant phospholipase A, Vicia faba",
author = "{Kyong Kim}, Dae and Hojoung Lee and Youngsook Lee",
year = "1994",
month = "5",
day = "2",
doi = "10.1016/0014-5793(94)80558-X",
language = "English",
volume = "343",
pages = "213--218",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Elsevier",
number = "3",

}

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 -