Transient occurrence of an ebulin-related d-galactose-lectin in shoots of Sambucus ebulus L.

详细信息    查看全文

• 作者：Lucí ; a Citores ; Marí ; a A. Rojo ; Pilar Jimé ; nez ; José ; M. Ferreras ; Rosario Iglesias ; Isabel Aranguez ; Tomá ; s Girbé ; s
• 关键词：Sambucus ebulus L. ; Dwarf elder ; Lectin ; SELlm ; Ricin ; Ebulin ; Ribosome-inactivating protein (RIP)
• 刊名：Phytochemistry
• 出版年：2008
• 出版时间：February 2008
• 年：2008
• 卷：69
• 期：4
• 页码：857-864
• 全文大小：822 K

文摘

Young shoots of Sambucus ebulus L. contain a monomeric d-galactose binding lectin (SELlm), which disappears upon shoot development, and was previously undetected since it co-purifies with the non-toxic type 2 ribosome-inactivating protein ebulin l and the dimeric lectin SELld. Molecular cloning of cDNA coding for SELlm and mass spectrometry analysis revealed a protein with a molecular mass of 34,239 Da, which displays 80 % , 77 % and 45 % of amino acid sequence identity with the ebulin l-B chain, SELld and ricin-B chain, respectively. Furthermore, the cloned precursor, with respect to the ebulin l precursor is truncated and contains the signal peptide, a piece of the A chain, a piece of the connecting peptide and the B chain. Further processing yields the lectin protein, which contains only the B chain. Despite the fact that SELlm displays the same d-galactose-binding sites than ricin, it was found that the lectin has different binding properties to d-galactose-containing matrix than ricin. Notably, and unlike ricin, the binding of SELlm and other Sambucus lectins to such matrix was maximum in range of 0–10 °C and abolished at 20 °C.