Russell-Jones G J, Ey P L, Reynolds B L
Aust J Exp Biol Med Sci. 1984 Feb;62 ( Pt 1):1-10. doi: 10.1038/icb.1984.1.
The polymeric and monomeric (7S) forms of the nitrophenyl-specific MOPC-315 murine IgA myeloma protein were examined for their capacity to inhibit the consumption of guinea-pig complement (C) by the C-activating protein DNP46BSA and by antigen-antibody (Ag-Ab) complexes. On a molar basis, 13S IgA was slightly (2-3 fold) more efficient than 7S IgA in inhibiting C consumption by DNP-BSA. When mixed with IgG antibodies prior to incubation with a non-complement-fixing antigen (TNP-KLH), 13S IgA was considerably more effective than 7S IgA in preventing the formation of Ag-Ab complexes able to fix C. The degree of inhibition observed was related to the concentration of C used in the assay, being greater at lower C concentrations.
对硝基苯基特异性的MOPC - 315鼠IgA骨髓瘤蛋白的聚合物形式和单体形式(7S)进行了检测,以考察它们抑制豚鼠补体(C)被C激活蛋白DNP46BSA以及抗原 - 抗体(Ag - Ab)复合物消耗的能力。以摩尔计,13S IgA在抑制DNP - BSA消耗C方面比7S IgA稍有效(2 - 3倍)。当在与非补体结合抗原(TNP - KLH)孵育之前与IgG抗体混合时,13S IgA在防止能够固定C的Ag - Ab复合物形成方面比7S IgA有效得多。观察到的抑制程度与测定中使用的C浓度有关,在较低C浓度时抑制作用更强。