A comparative study of bark lectins from three elderberry (Sambucus) species.
A comparative study of bark lectins from three elderberry (Sambucus) species.
复制标题
DOI：
10.1093/oxfordjournals.jbchem.a122972
复制
发表时间：
1989-12
影响因子：
2.7
通讯作者：
N. Shibuya;K. Tazaki;Zhiwei Song;G. Tarr;I. Goldstein;W. Peumans
中科院分区：
文献类型：
--
作者：
N. Shibuya;K. Tazaki;Zhiwei Song;G. Tarr;I. Goldstein;W. Peumans
从欧洲接骨木属接骨木属三种植物的树皮中分离得到三种接骨木凝集素。nigra）、北美（S. canadensis）和日本（S. sieboldiana）的碳水化合物结合特性和一些结构特征进行了比较研究。所有三种凝集素每个分子都含有两个相同的碳水化合物结合位点，并且对Neu 5Ac（α 2-6）-Gal/GalNAc序列显示出非常高的特异性。然而，各种寡糖的相对亲和力显着不同，这表明这些凝集素的碳水化合物结合位点的详细结构的差异。这三种凝集素在免疫学上是相关的，但不相同，并且都由疏水和亲水亚基区域组成，尽管这些亚基的分子大小在三种凝集素之间略有不同。这些凝集素的亚基的N-末端序列分析表明，它们在该区域具有非常相似的结构，但也表明N-末端加工的发生，例如所有三种凝集素的疏水和亲水亚基的N-末端处的几个氨基酸残基的缺失。三种凝集素的胰蛋白酶肽图谱显示了所有凝集素的相似模式，但也显示了每种凝集素存在一些独特的肽。
Three elderberry lectins isolated from the bark of three different species of the genus Sambucus which are native to Europe (S. nigra), North America (S. canadensis), and Japan (S. sieboldiana) were studied comparatively with regard to their carbohydrate binding properties and some structural features. All three lectins contained two identical carbohydrate binding sites per molecule and showed a very high specificity for the Neu5Ac(alpha 2-6)-Gal/GalNAc sequence. However, relative affinities for various oligosaccharides were significantly different among them, suggesting differences in the detailed structure of the carbohydrate binding sites of these lectins. The three lectins were immunologically related, but not identical, and all were composed of hydrophobic and hydrophilic subunit regions, although the molecular sizes of these subunits were slightly different among the three lectins. N-terminal sequence analysis of the subunits of these lectins suggested that they have a very similar structure in this region but also indicated the occurrence of N-terminal processing such as the deletion of several amino acid residues at the N-termini for both hydrophobic and hydrophilic subunits of all three lectins. Tryptic peptide mapping of the three lectins showed a similar pattern for all of them but also showed the presence of some unique peptides for each lectin.