Kondoh H, Kobayashi K
Department of Pediatrics, Yamaguchi University School of Medicine, Japan.
Clin Chim Acta. 1988 May 13;174(1):15-23. doi: 10.1016/0009-8981(88)90363-4.
Jackfruit lectin, jacalin, has been characterized to combine with IgA of only IgA1 subclass but not with IgA2 subclass and other immunoglobulins. However, we found in the present study that a lectin from another batch of jackfruit (Jacalin-H) showed a different nature in binding reaction. Jacalin-H combined with immunoglobulins of every class or subclass except monomer IgG. More interestingly, the Jacalin-H also combined with aggregated IgG. By means of the Jacalin-H affinity chromatography, we could efficiently eliminate aggregated IgG as well as immunoglobulins other than monomer IgG from commercial gamma-globulin preparations. Jacalin-H affinity chromatography is easy, inexpensive and efficient in the elimination of undesirable immunoglobulin contaminants in the commercial gamma-globulin preparations.
波罗蜜凝集素,即jacalin,已被鉴定为仅与IgA1亚类的IgA结合,而不与IgA2亚类及其他免疫球蛋白结合。然而,我们在本研究中发现,另一批波罗蜜中的一种凝集素(Jacalin-H)在结合反应中表现出不同的特性。Jacalin-H能与除单体IgG外的各类或亚类免疫球蛋白结合。更有趣的是,Jacalin-H还能与聚集的IgG结合。通过Jacalin-H亲和层析,我们能够从商业γ球蛋白制剂中有效去除聚集的IgG以及单体IgG以外的免疫球蛋白。Jacalin-H亲和层析在去除商业γ球蛋白制剂中不需要的免疫球蛋白污染物方面简便、廉价且高效。