Kane P, Holowka D, Baird B
Department of Chemistry, Cornell University, Ithaca, NY 14853-1301.
Immunol Invest. 1990 Feb;19(1):1-25. doi: 10.3109/08820139009042022.
Model antigens of defined structure and limited valency have been prepared by binding 2,4-dinitrophenyl (DNP)-biotin haptens of different lengths to the biotin binding sites of avidin. These complexes have been characterized structurally by spectroscopic methods and functionally by testing their ability to crosslink cell-bound anti-DNP immunoglobulin E-receptor complexes to stimulate degranulation of rat basophilic leukemia cells. One of these haptens, 1-DNP-amino-12-biotinamido dodecane, is shown to have only two tight binding sites per avidin molecule, and the resulting bivalent (DNP-biotin)-avidin antigen is found to stimulate substantial degranulation. Another DNP-biotin hapten that is approximately 10 A longer has four tight binding sites per avidin and, when bound to avidin, has greater activity similar to a highly DNP-conjugated multivalent antigen. These and other (DNP-biotin)-avidin complexes described here represent a new group of chemically well-defined antigens that are useful for studying the binding to and functional crosslinking of cell-bound immunoglobulins in immunological responses.
通过将不同长度的2,4-二硝基苯基（DNP）-生物素半抗原与抗生物素蛋白的生物素结合位点结合，制备了具有确定结构和有限价态的模型抗原。这些复合物已通过光谱方法进行结构表征，并通过测试它们交联细胞结合的抗DNP免疫球蛋白E受体复合物以刺激大鼠嗜碱性白血病细胞脱颗粒的能力进行功能表征。其中一种半抗原，1-DNP-氨基-12-生物素酰胺十二烷，显示每个抗生物素蛋白分子只有两个紧密结合位点，并且发现所得的二价（DNP-生物素）-抗生物素蛋白抗原能刺激大量脱颗粒。另一种比其长约10埃的DNP-生物素半抗原每个抗生物素蛋白有四个紧密结合位点，并且当与抗生物素蛋白结合时，具有与高度DNP偶联的多价抗原相似的更大活性。本文所述的这些以及其他（DNP-生物素）-抗生物素蛋白复合物代表了一组新的化学定义明确的抗原，可用于研究免疫反应中细胞结合免疫球蛋白的结合和功能交联。
