Puri N, Augusteyn R C, Owen E A, Siezen R J
Eur J Biochem. 1983 Aug 1;134(2):321-6. doi: 10.1111/j.1432-1033.1983.tb07569.x.
A competitive radioimmunoassay was used to determine the reactivities of alpha-crystallins from 13 species with antibodies directed toward calf alpha-crystallin. The results indicate that species as diverse as human and dogfish share the same number of crossreacting antigenic determinants. The various alpha-crystallins can be distinguished only on the basis of their differing affinities for the antiserum. Hydrophilicity profiles for alpha A and alpha B polypeptides of all species were found to be remarkably similar. On the basis of these, four major sequential determinants could be predicted for each polypeptide. The location and sequence of these determinants were found to be essentially conserved in all alpha-crystallins examined. These results are in agreement with the observed crossreactivities. However, there was little obvious correlation between substitutions in determinants and observed variations in respective alpha-crystallin/antibody affinities. Conservation of antigenic determinants over such a wide evolutionary range may reflect stringent constraints on the overall surface and three-dimensional structure of vertebrate alpha-crystallins.
采用竞争性放射免疫测定法，以针对小牛α-晶体蛋白的抗体来测定13个物种的α-晶体蛋白的反应活性。结果表明，人类和狗鱼等差异极大的物种具有相同数量的交叉反应抗原决定簇。各种α-晶体蛋白只能根据它们与抗血清的不同亲和力来区分。发现所有物种的αA和αB多肽的亲水性图谱非常相似。基于此，可以预测每种多肽有四个主要的连续决定簇。这些决定簇的位置和序列在所有检测的α-晶体蛋白中基本保守。这些结果与观察到的交叉反应性一致。然而，决定簇中的取代与各自α-晶体蛋白/抗体亲和力的观察变化之间几乎没有明显的相关性。在如此广泛的进化范围内抗原决定簇的保守性可能反映了对脊椎动物α-晶体蛋白整体表面和三维结构的严格限制。
