Singh J, Kamboj K K, Kamboj S S, Shangary S, Sandhu R S
Department of Molecular Biology and Biochemistry, Guru Nanak Dev University, Amritsar, India.
Ital J Biochem. 1994 Sep-Oct;43(5):207-18.
Asialofetuin-linked amino activated silica was used for the affinity purification of lectins from Amaranthus hypochondriacus Linn (AHL) and A. tricolor Linn (ATL). Like a few other Amaranthus lectins, these lectins were also inhibited by N-acetyl-D-galactosamine, fetuin and asialofetuin; they agglutinated human and different animal erythrocytes. The purified lectins yielded a single band on PAGE pH 8.3, pH 4.5 and SDS-PAGE, pH 8.3. These also gave a single peak in gel exclusion on Biogel P-200, HPLC 300 SW and cation exchange columns. However, both lectins gave multiple peaks in anion exchange column and multiple bands in isoelectric focusing. AHL and ATL are dimeric proteins in which the subunits having M(r) 29,000 and 39,000, respectively, are not held together by disulphide linkages. The pure lectins are glycoproteins and do not require Ca2+, Mn2+ and Mg2+ for their agglutination activity.
用唾液酸胎球蛋白连接的氨基活化硅胶从皱果苋（AHL）和三色苋（ATL）中亲和纯化凝集素。与其他一些苋属凝集素一样，这些凝集素也被N-乙酰-D-半乳糖胺、胎球蛋白和唾液酸胎球蛋白抑制；它们能凝集人和不同动物的红细胞。纯化后的凝集素在pH 8.3、pH 4.5的聚丙烯酰胺凝胶电泳（PAGE）以及pH 8.3的十二烷基硫酸钠聚丙烯酰胺凝胶电泳（SDS-PAGE）上均呈现单一条带。在Biogel P-200、高效液相色谱300 SW和阳离子交换柱上进行凝胶排阻时，它们也都给出单一峰。然而，这两种凝集素在阴离子交换柱上给出多个峰，在等电聚焦中呈现多条带。AHL和ATL是二聚体蛋白，其中亚基的相对分子质量分别为29,000和39,000，它们不是通过二硫键连接在一起的。纯凝集素是糖蛋白，其凝集活性不需要Ca2+、Mn2+和Mg2+。
