Nespoulous C, Gaudemer O, Huet J C, Pernollet J C
Unité de Recherches de Biochimie et Structure des Protéines, INRA, Jouy-en-Josas, France.
FEBS Lett. 1999 Jun 11;452(3):400-6. doi: 10.1016/s0014-5793(99)00654-7.
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.
植物致病卵菌辣椒疫霉在培养过程中分泌一种磷脂酶活性物质。通过色谱法和电泳法分离出了两种具有高磷脂酶B活性的酶同工型。它们的表观摩尔质量不同（分别为22 kDa和32 kDa）。这两种蛋白质都进行了糖基化修饰，并且在第39个残基之前具有相同的N端氨基酸序列，与辣椒疫霉激发子辣椒素具有高度同源性。尽管辣椒素没有磷脂酶活性，但圆二色性显示它能与带负电荷的磷脂特异性相互作用，这表明膜脂可能是激发子的潜在靶点。
