Darsley M J, Rees A R
EMBO J. 1985 Feb;4(2):383-92. doi: 10.1002/j.1460-2075.1985.tb03640.x.
Five monoclonal antibodies specific for the loop region of hen egg lysozyme were prepared by immunisation with a synthetic conjugate of a proteolytic fragment of lysozyme coupled to bovine serum albumin. Their fine specificities were investigated using a panel of variant lysozymes and peptide fragments of lysozyme in a quantitative radio-immunoassay procedure. Knowledge of the structure of hen lysozyme to high resolution and the use of computer graphics enables the localisation of the epitopes recognised by the antibodies with some precision. The antibodies were shown to define three distinct, overlapping epitopes within what was previously considered to be a single antigenic site. These results are discussed in relation to current ideas of the antigenic nature of proteins and other recent studies in which anti-protein antibodies have been elicited by immunisation with small peptides.
通过用溶菌酶蛋白水解片段与牛血清白蛋白的合成偶联物免疫制备了五种对鸡蛋清溶菌酶环区具有特异性的单克隆抗体。使用一组溶菌酶变体和溶菌酶肽片段，通过定量放射免疫分析程序研究了它们的精细特异性。对鸡溶菌酶高分辨率结构的了解以及计算机图形学的应用使得能够较为精确地定位抗体识别的表位。结果表明，这些抗体在先前被认为是单一抗原位点的区域内定义了三个不同的、重叠的表位。结合当前关于蛋白质抗原性质的观点以及其他近期通过用小肽免疫引发抗蛋白质抗体的研究，对这些结果进行了讨论。
