Format

Send to

Choose Destination
FEBS Lett. 1999 Jun 11;452(3):400-6.

Characterization of elicitin-like phospholipases isolated from Phytophthora capsici culture filtrate.

Author information

1
Unité de Recherches de Biochimie et Structure des Protéines, INRA, Jouy-en-Josas, France. nespoulo@jouy.inra.fr

Abstract

The phytopathogenic oomycete Phytophthora capsici secretes 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. capsici elicitin. 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.

PMID:
10386629
DOI:
10.1016/s0014-5793(99)00654-7
[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for Wiley
Loading ...
Support Center