Adinolfi A, Massa O, d'Alessandro G
International Institute of Genetics and Biophysics, CNR, Naples, Italy.
Ann Hum Genet. 1986 Jul;50(3):197-206. doi: 10.1111/j.1469-1809.1986.tb01039.x.
Rabbit immune sera raised against denatured forms of horse liver alcohol dehydrogenase and of human ADH5 isozyme were found to react with the denatured subunits of all the human ADH isozymes regardless of their class. The immune serum against the human ADH isozyme cross-reacted also with horse ADH subunits and, at appropriate dilutions, both the immune sera reacted with denatured yeast ADH, suggesting that common structures have been preserved in these molecules over a long evolutionary period. The immune sera partially reacted also with the respective antigens in their native conformation, indicating that some 'sequential' epitopes are expressed on the surface of the folded proteins.
针对马肝乙醇脱氢酶变性形式和人ADH5同工酶产生的兔免疫血清，被发现能与所有人类ADH同工酶的变性亚基发生反应，而不论其类别如何。针对人ADH同工酶的免疫血清也与马ADH亚基发生交叉反应，并且在适当稀释时，两种免疫血清都与变性酵母ADH发生反应，这表明在漫长的进化过程中，这些分子中保留了共同的结构。免疫血清也与各自天然构象的抗原部分发生反应，表明一些“连续”表位在折叠蛋白的表面表达。
