Lipinski M, Nudelman E D, Wiels J, Parsons M
J Immunol. 1982 Nov;129(5):2301-4.
Monoclonal antibody 38.13 detects an epitope presented on Burkitt's lymphoma cells that has not been detected on other lymphoid tissues or tumors. The biochemical nature of this Burkitt's lymphoma-associated antigen was investigated by staining inhibition assays. Indirect immunofluorescence and fluorescence-activated cell sorter analysis show that antibody 38.13 reacts with a protease-resistant structure present among the hydrophobic components extracted with chloroform-methanol from the Ramos Burkitt's cell line. These components were further separated by ion-exchange chromatography and activity resides in the unbound (neutral) fraction. The staining antibody is specifically absorbed when preincubated with D-galactose, and to a lesser extent with N-acetyl-galactosamine. Therefore, 38.13 appears to recognize a determinant of carbohydrate nature, which is carried on a neutral glycolipid.
单克隆抗体38.13可检测到伯基特淋巴瘤细胞上呈现的一种表位,而在其他淋巴组织或肿瘤上尚未检测到该表位。通过染色抑制试验研究了这种与伯基特淋巴瘤相关抗原的生化性质。间接免疫荧光和荧光激活细胞分选分析表明,抗体38.13与用氯仿 - 甲醇从拉莫斯伯基特细胞系中提取的疏水成分中存在的一种抗蛋白酶结构发生反应。这些成分通过离子交换色谱进一步分离,活性存在于未结合(中性)部分。当与D - 半乳糖预孵育时,染色抗体被特异性吸收,与N - 乙酰半乳糖胺的吸收程度较小。因此,38.13似乎识别一种碳水化合物性质的决定簇,该决定簇存在于中性糖脂上。