Characterization of elicitin‐like phospholipases isolated from Phytophthora capsiciculture filtrate

Autor: Nespoulous, Claude, Gaudemer, Odile, Huet, Jean-Claude, Pernollet, Jean-Claude
Zdroj: FEBS Letters; June 1999, Vol. 452 Issue: 3 p400-406, 7p
Abstrakt: The phytopathogenic oomycete Phytophthora capsicisecretes in culture a phospholipase activity. Two enzyme isoforms exhibiting a high phospholipase B activity were isolated by chromatography and electrophoresis. They differ in their apparent molar masses (22 and 32 kDa). Both proteins are glycosylated and share the same N‐terminal amino acid sequence up to the 39th residue with a high homology with capsicein, the P. capsicielicitin. Although devoid of phospholipase activity, capsicein was shown by circular dichroism to specifically interact with negatively charged phospholipids, suggesting that the membrane lipids could be a potential target for elicitins.
Databáze: Supplemental Index