Sandilands G P, Reid F M, O'Keeffe T, Peel M G
J Immunol Methods. 1980;36(1):1-11. doi: 10.1016/0022-1759(80)90089-7.
Soluble transferrin-anti-transferrin (TAT) complexes were shown by EA-rosette inhibition assay to block human lymphocyte receptors for the Fc of reacted IgG (Fc gamma) in vitro. These complexes, which provide a convenient and controlled source of Fc gamma receptor blocking material, were found to inhibit EA-rosette formation over a wide range of antigen: antibody ratios. Complexes were detected at both 37 degrees C and 4 degrees C although the range and sensitivity of the assay was markedly increased at 4 degrees C. The inhibitory capacity of TAT complexes was lost on pre-incubation with normal human serum suggesting that only non-complement fixing complexes are detected by EA-rosette inhibition. "False positive" inhibition by antilymphocyte antibodies occurs at 37 degrees C but not at 4 degrees C. Partial automation of the assay was achieved by calibrating a Coulter counter for rosette counting, thus obviating the requirement for tedious and subjective microscopic determinations.
通过EA花环抑制试验表明,可溶性转铁蛋白 - 抗转铁蛋白(TAT)复合物在体外可阻断人淋巴细胞上与反应性IgG(Fcγ)的Fc结合的受体。这些复合物提供了一种方便且可控的Fcγ受体阻断物质来源,发现在广泛的抗原:抗体比例范围内均可抑制EA花环的形成。在37℃和4℃均检测到复合物,尽管在4℃时该试验的范围和灵敏度显著提高。TAT复合物与正常人血清预温育后其抑制能力丧失,这表明EA花环抑制试验仅检测到非补体结合复合物。抗淋巴细胞抗体在37℃时会出现“假阳性”抑制,但在4℃时不会。通过校准库尔特计数器进行花环计数实现了该试验的部分自动化,从而无需进行繁琐且主观的显微镜检测。