Hankins C N, Kindinger J, Shannon L M
Department of Biochemistry, University of California, Riverside, California 92521.
Plant Physiol. 1987 Apr;83(4):825-9. doi: 10.1104/pp.83.4.825.
Two lectins, Leaf Lectin I and Leaf Lectin II (LLI and LLII) were purified from the leaves of Sophora japonica. Like the Sophora seed lectin, LLI and LLII are tetrameric glycoproteins containing a single subunit with respect to size. The subunits of LLI (32 kilodaltons) and LLII (34 kilodaltons) are slightly larger than those of the seed lectin (29.5 kilodaltons). The three Sophora lectins display indistinguishable specificities, amino acid compositions, specific hemagglutinin activities, and extinction coefficients. Although very closely related to the seed lectin, the leaf and seed lectins are not immunologically identical and they differ in subunit molecular weights, carbohydrate content, and in the pH sensitivity of their hemagglutinin activities. N-terminal amino acid sequence analysis shows that although they are homologous proteins, the three Sophora lectins are products of distinct genes.
从槐树叶片中纯化出了两种凝集素，即叶片凝集素I和叶片凝集素II（LLI和LLII）。与槐豆凝集素一样，LLI和LLII是四聚体糖蛋白，就大小而言含有单个亚基。LLI（32千道尔顿）和LLII（34千道尔顿）的亚基比种子凝集素的亚基（29.5千道尔顿）略大。这三种槐树凝集素表现出难以区分的特异性、氨基酸组成、特定的血凝活性和消光系数。尽管叶片凝集素与种子凝集素密切相关，但它们在免疫上并不相同，并且在亚基分子量、碳水化合物含量以及血凝活性的pH敏感性方面存在差异。N端氨基酸序列分析表明，尽管这三种槐树凝集素是同源蛋白，但它们是不同基因的产物。
