Hoffman D R
J Allergy Clin Immunol. 1986 Aug;78(2):337-43. doi: 10.1016/s0091-6749(86)80086-0.
Phospholipases (PLs) isolated from the venoms of three species of yellow jackets, white-faced hornets, European hornets, and paper wasps were studied by peptide mapping after limited enzyme hydrolyses and cyanogen bromide cleavage. Significant differences in the primary structures were observed. Cross-reactivities of vespid PLs were studied by precipitation reactions in gel with rabbit antibodies, immunoblots of sodium dodecyl sulfate-polyacrylamide gel electrophoresis gels with rabbit antisera, and RAST inhibition with individual sera from vespid-reactive patients. The cross-reactivities of both human IgE antibodies and rabbit IgG antibodies were variable and not reciprocal between antigen and antibody, suggesting that there are multiple antigenic determinants on the PL molecules and that individuals respond to different determinants. No general patterns of cross-reactivity could be observed.
通过有限酶水解和溴化氰裂解后的肽图谱分析，对从三种黄夹克、白面大黄蜂、欧洲大黄蜂和胡蜂毒液中分离出的磷脂酶（PLs）进行了研究。观察到其一级结构存在显著差异。通过用兔抗体在凝胶中进行沉淀反应、用兔抗血清对十二烷基硫酸钠 - 聚丙烯酰胺凝胶电泳凝胶进行免疫印迹以及用来自对胡蜂有反应的患者的个体血清进行放射变应原吸附试验（RAST）抑制，研究了胡蜂PLs的交叉反应性。人IgE抗体和兔IgG抗体的交叉反应性都是可变的，并且抗原与抗体之间不是相互的，这表明PL分子上存在多个抗原决定簇，而且个体对不同的决定簇有反应。未观察到交叉反应性的一般模式。
