Kabir S, Ahmed I S, Daar A S
Department of Surgery, College of Medicine, Sultan Qaboos University, Oman.
Immunol Invest. 1995 Aug;24(5):725-35. doi: 10.3109/08820139509060701.
Rabbit immunoglobulin G (IgG) was subjected to affinity chromatography on a column of jacalin-Sepharose 4B. While the majority of IgG molecules did not bind, a small fraction, representing about 25% of the total IgG applied, bound to jacalin-Sepharose 4B. The binding of rabbit IgG to jacalin was further evidenced by ELISA performed on jacalin coated microtitre plates. While the jacalin-retained IgG fraction displayed strong binding, the unretained fraction did not demonstrate any detectable binding. Upon SDS-PAGE, both the jacalin retained and unretained rabbit IgG fractions displayed identical protein profiles. Upon protein blotting it was demonstrated that jacalin binding sites were located only on the heavy chain of IgG. These results suggest that rabbit IgG molecules are heterogeneous with respect to their glycosylation patterns. A small fraction of rabbit IgG molecules binds jacalin and the process is probably mediated through O-linked oligosaccharides present on the heavy chain of IgG.
将兔免疫球蛋白G（IgG）在红豆蔻凝集素-琼脂糖4B柱上进行亲和层析。虽然大多数IgG分子不结合，但一小部分（约占所加总IgG的25%）与红豆蔻凝集素-琼脂糖4B结合。在包被有红豆蔻凝集素的微量滴定板上进行的酶联免疫吸附测定（ELISA）进一步证明了兔IgG与红豆蔻凝集素的结合。虽然被红豆蔻凝集素保留的IgG部分显示出强结合，但未被保留的部分未显示出任何可检测到的结合。在十二烷基硫酸钠-聚丙烯酰胺凝胶电泳（SDS-PAGE）中，被红豆蔻凝集素保留和未被保留的兔IgG部分显示出相同的蛋白质谱。在蛋白质印迹分析中表明，红豆蔻凝集素结合位点仅位于IgG的重链上。这些结果表明，兔IgG分子在糖基化模式方面是异质的。一小部分兔IgG分子结合红豆蔻凝集素，该过程可能是通过IgG重链上存在的O-连接寡糖介导的。
