REAL-TIME ANALYSIS OF ANTIBODY ANTIGEN REACTION-KINETICS
REAL-TIME ANALYSIS OF ANTIBODY ANTIGEN REACTION-KINETICS
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DOI：
10.1111/j.1365-3083.1992.tb02970.x
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发表时间：
1992-06-01
影响因子：
3.7
通讯作者：
BORREBAECK, CAK
中科院分区：
文献类型：
--
作者：
MALMBORG, AC;MICHAELSSON, A;BORREBAECK, CAK
表面等离子体共振。即检测表面上折射率的变化，用于生物传感器中以评估人单克隆IgG和IgM抗体以及Fab片段的解离/结合速率和亲和常数。结果表明，观察到的完整和片段IgG抗破伤风抗体之间亲和力常数的差异与解离速率常数的约10倍差异有关，因为结合速率常数在相同范围内，即2-3 x 10（5）（M-1 s-1）。亲和常数，由传统的固相酶免疫测定法测定，基本上高于由生物传感器产生的常数。人单克隆IgM抗Tn-α抗体显示。与IgG抗体相比，结合速率常数高一个数量级，但因为解离速率常数高十倍以上。所得抗碳水化合物IgM抗体的亲和常数仍略低于IgG抗体的亲和常数。
Surface plasmon resonance. i.e. detection of changes in refractive index on a surface, was used in a biosensor to evaluate the dissociation/association rate and affinity constants of human monoclonal IgG and IgM antibodies and Fab fragments. The results showed that an observed difference in affinity constants between intact and fragmented IgG anti-tetanus antibody was related to approximately 10-fold differences in dissociation rate constants, since the association rate constants were in the same range, i.e. 2-3 x 10(5) (M-1 s-1). Affinity constants, as determined by conventional solid phase enzyme immunoassays, were substantially higher than the constants produced by the biosensor. Human monoclonal IgM anti-Tn-alpha antibodies showed, furthermore. one order of magnitude higher association rate constants, as compared with the IgG antibodies, but since the dissociation rate constants were more than ten times higher. the resulting affinity constants of the anti-carbohydrate IgM antibodies were still somewhat lower than those of the IgG antibodies.