Fritz R B, Chou C H
J Immunol. 1983 May;130(5):2180-2.
Two monoclonal antibodies, one raised by immunization with mouse myelin basic protein (MBP) and the second raised by immunization with peptide 68-88 of guinea pig MBP, were compared with respect to specificity. The former antibody (15.32) cross-reacted completely with rat, guinea pig, human, and bovine MBP. It also reacted with peptide 43-88 from each MBP. The latter antibody (22.17) was nonreactive with MBP, but cross-reacted with peptide 43-88 from rat, human, guinea pig, and bovine MBP. When tested with small peptides derived from peptide 43-88, antibody 22.17 reacted with an epitope in the C-terminal region. Antibody 15.32 reacted with an epitope in the N-terminal half of the peptide. The data show that 22.17 reacted with a unique epitope associated only with free peptide, whereas 15.32 recognized an epitope common to both peptide 43-88 and MBP.
比较了两种单克隆抗体的特异性，一种是通过用小鼠髓鞘碱性蛋白（MBP）免疫制备的，另一种是通过用豚鼠MBP的68 - 88肽段免疫制备的。前一种抗体（15.32）与大鼠、豚鼠、人及牛的MBP完全交叉反应。它也与每种MBP的43 - 88肽段发生反应。后一种抗体（22.17）与MBP无反应，但与大鼠、人、豚鼠及牛的MBP的43 - 88肽段交叉反应。当用源自43 - 88肽段的小肽进行检测时，抗体22.17与C末端区域的一个表位发生反应。抗体15.32与该肽段N末端一半的一个表位发生反应。数据表明，22.17与仅与游离肽相关的独特表位发生反应，而15.32识别43 - 88肽段和MBP共有的一个表位。
