Ghetie M A, Margineanu M, Ghetie V
J Immunol Methods. 1986 Mar 13;87(2):239-44. doi: 10.1016/0022-1759(86)90537-5.
Ricinus communis agglutinin covalently bound to Sepharose 4B (RcA-Sepharose 4B) was able to selectively bind immune complexes consisting of antigen (bovine serum albumin) and rabbit IgG antibody which were rich in antibody (i.e., high molecular weight complexes of approximately 2000 000). No interaction was recorded between RcA-Sepharose 4B and immune complexes consisting of the antigen plus rabbit IgG antibody which were rich in antigen (i.e., complexes with a molecular weight of 300 000-500 000). These results indicate that binding to RcA is due to the increased density of galactose residues in the high molecular weight polymeric antibody component of the soluble immune complexes.
共价结合到琼脂糖4B上的蓖麻凝集素（RcA-琼脂糖4B）能够选择性结合由抗原（牛血清白蛋白）和兔IgG抗体组成的免疫复合物，这些免疫复合物富含抗体（即分子量约为2000000的高分子量复合物）。未观察到RcA-琼脂糖4B与由抗原加兔IgG抗体组成的富含抗原的免疫复合物（即分子量为300000 - 500000的复合物）之间有相互作用。这些结果表明，与RcA的结合是由于可溶性免疫复合物的高分子量聚合抗体成分中半乳糖残基密度增加所致。
