Rearden A, Masouredis S P
Transfusion. 1980 Jul-Aug;20(4):377-83. doi: 10.1046/j.1537-2995.1980.20480260268.x.
The quantity of anti-IgG bound at equilibrium to cell-bound anti-D failed to increase with enzymatic modification of intact red blood cells. This contrasts with results obtained by immunoelectronmicroscopy with unsealed red blood cell ghosts. Ghosts derived from enzyme-modified, anti-D-sensitized intact red blood cells show an increased ratio of anti-IgG to anti-D. The ratio declined with protease modification of intact cells, possibly because of steric hinderance to anti-IgG binding within the cellular agglutinates. At comparable levels of cell-bound anti-D and anti-IgG, enzyme-modified cells were more agglutinable in the antiglobulin reaction than unmodified cells. As in saline hemagglutination, enzymatic enhancement of agglutinability appears to be unrelated to the amount of antibody bound, but rather may be related to other factors such as alterations of the biophysical properties of the red blood cell membrane.
与完整红细胞经酶修饰后相比，平衡时与细胞结合的抗 - D结合的抗 - IgG量并未增加。这与用未封闭的红细胞血影进行免疫电子显微镜观察得到的结果形成对比。源自酶修饰、抗 - D致敏的完整红细胞的血影显示抗 - IgG与抗 - D的比例增加。完整细胞经蛋白酶修饰后该比例下降，这可能是由于细胞凝集物中抗 - IgG结合存在空间位阻。在细胞结合的抗 - D和抗 - IgG水平相当的情况下，酶修饰的细胞在抗球蛋白反应中比未修饰的细胞更易凝集。与盐水血凝反应一样，凝集性的酶促增强似乎与结合的抗体量无关，而可能与其他因素有关，如红细胞膜生物物理性质的改变。
