Yao Z J, Kao M C, Loh K C, Chung M C
Bioprocessing Technology Unit, National University of Singapore, Republic of Singapore.
Biochem Mol Biol Int. 1994 Apr;32(5):951-9.
Human lymphotoxin (hLT or TNF-beta) is a lymphokine that is structurally and functionally related to tumor necrosis factor alpha (TNF-alpha). The continuous epitopes of hLT were located by examining the cross-reaction between rabbit anti-hLT antibody and peptides derived from proteolytic digestion and chemical synthesis. Three antigenic sites, corresponding to residues 40-48, 83-94 and 139-147, of the protein sequence, were located by this approach. Since residues 49-57 also exhibited trace antigenicity, but residues 45-52 displayed no reaction, the whole peptide fragment consisting of residues 40-57 might be necessary for antigenicity. A comparison of the antigenic determinants with the loop structures obtained from X-ray crystallographic studies of hLT showed that all of the epitopes are found on or adjacent to functionally important domains.
人淋巴毒素（hLT或肿瘤坏死因子-β）是一种淋巴因子，在结构和功能上与肿瘤坏死因子-α（TNF-α）相关。通过检测兔抗hLT抗体与蛋白酶消化和化学合成产生的肽之间的交叉反应，确定了hLT的连续表位。通过这种方法，确定了该蛋白质序列中对应于第40 - 48、83 - 94和139 - 147位残基的三个抗原位点。由于第49 - 57位残基也表现出微量抗原性，但第45 - 52位残基无反应，因此由第40 - 57位残基组成的整个肽片段可能对抗原性是必需的。将抗原决定簇与通过hLT的X射线晶体学研究获得的环结构进行比较，结果表明所有表位均位于功能重要结构域上或其附近。
