Foutain D W, Yang W K
Biochim Biophys Acta. 1977 May 27;492(1):176-85. doi: 10.1016/0005-2795(77)90224-0.
The major lectin in seeds of a soybean cultivar (Glycine max cv D68-127) has been purified to apparent homogeneity by hydroxyapatite and DEAE-cellulose chromatography. In the latter, the behavior of the lectin was similar to that of the minor isolectins previously described in other soybean cultivars. Molecular weights of 92 000 for the molecule and 23 000 for the subunits were determined by gel filtration and sodium dodecyl sulfate-gel electrophoresis; these are smaller than those previously reported for the major lectin in another soybean variety. Hemagglutination by the lectin was inhibited specifically by N-acetyl-D-galactosamine and galactose-containing sugars.
通过羟基磷灰石和二乙氨基乙基纤维素色谱法,已将一个大豆品种(大豆品种D68 - 127)种子中的主要凝集素纯化至表观均一。在后者中,该凝集素的行为与先前在其他大豆品种中描述的次要同工凝集素相似。通过凝胶过滤和十二烷基硫酸钠 - 凝胶电泳测定该分子的分子量为92000,亚基的分子量为23000;这些数值比先前报道的另一个大豆品种中的主要凝集素的分子量要小。该凝集素的血细胞凝集作用被N - 乙酰 - D - 半乳糖胺和含半乳糖的糖类特异性抑制。