Kennedy J F, Keep P A, Catty D
J Immunol Methods. 1982;50(1):57-75. doi: 10.1016/0022-1759(82)90304-0.
Cellulose trans-2,3-carbonate has been used as a new insoluble matrix for the simple coupling of a1- and b4-positive rabbit immunoglobulin to make immunoadsorbents capable of purifying from serum, with great efficiency, alloantibodies to these allotypic determinants. The antibodies have themselves been conjugated to prepare specific antibody immunoadsorbents of high binding activity for their allotypic target molecules. With these anti-allotypic solid-phase reagents it has been possible to affinity purify a1- and b4-positive immunoglobulin molecules and to deplete serum immunoglobulin of these molecules to leave in the eluates only the allotypically uncontaminated minor immunoglobulin components which are a-negative or b-negative (lambda chain-bearing) molecules. lambda chain molecules were also purified in very small quantities by affinity chromatography on a sheep anti-rabbit lambda chain column. This method of purifying minor populations of rabbit immunoglobulin from normal serum by special immunoadsorbent applications offers new opportunities to study the products of rarely expressed immunoglobulin genes in normal rabbits.
纤维素反式 -2,3 - 碳酸酯已被用作一种新的不溶性基质，用于简单偶联α1和β4阳性兔免疫球蛋白，以制备能够高效从血清中纯化针对这些同种异型决定簇的同种抗体的免疫吸附剂。这些抗体本身已被偶联，以制备对其同种异型靶分子具有高结合活性的特异性抗体免疫吸附剂。使用这些抗同种异型固相试剂，已能够亲和纯化α1和β4阳性免疫球蛋白分子，并从血清免疫球蛋白中去除这些分子，使得洗脱液中仅留下无同种异型污染的次要免疫球蛋白成分，即α阴性或β阴性（含λ链）分子。λ链分子也通过在羊抗兔λ链柱上的亲和色谱法进行了极少量的纯化。这种通过特殊免疫吸附剂应用从正常血清中纯化少量兔免疫球蛋白的方法，为研究正常兔中罕见表达的免疫球蛋白基因的产物提供了新的机会。
