Antigens and allergens in Dermatophagoïdes farinae mite. I. Immunochemical and physicochemical study of two allergenic fractions from a partially-purified Dermatophagoïdes farinae mite extract.
Antigens and allergens in Dermatophagoïdes farinae mite. I. Immunochemical and physicochemical study of two allergenic fractions from a partially-purified Dermatophagoïdes farinae mite extract.
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粉尘螨中的抗原和过敏原 I. 部分纯化的粉尘螨提取物中两种过敏性组分的免疫化学和物理化学研究。
作者：
J. Le Mao;J. Dandeu;J. Rabillon;M. Lux;B. David
已通过凝胶过滤对粉尘螨培养物的部分纯化提取物进行分级。分离两个级分。P25是一个富含蛋白质的组分，分子量为100。约25，000。另一个是GP8，是一个富含多糖的级分，摩尔比为1：1。大约8000人。通过交叉免疫电泳，我们在部分纯化的透析液中检测到11种抗原。花粉提取物（Df 80d）以及P25组分中的活性。其中之一，ag 11，似乎是最重要的过敏原，因为在交叉放射免疫电泳实验中，它显示出更快的放射染色，这意味着它结合了最大部分的螨特异性IgE存在于一个池的螨敏感的患者的血清。通过交叉线免疫电泳，我们证明了在GP8中没有Ag 11，其中只有Ag 5和Ag 6是可识别的。放射性吸附试验（RAST）发现，P25和GP8包被的纸片可固定大多数D.粉尘敏感患者。将“主要过敏原”定义为大多数敏感患者产生特异性IgE的过敏原，P25和GP8似乎都含有至少一种主要过敏原。以Df 80 d为固相，采用RAST抑制法，发现P25的致敏活性略高于Df 80 d，而GP 8的抑制活性很弱。因此，GP8的过敏特异性不同于Df 80 d或P25。
The fractionation of a partially-purified extract of Dermatophagoïdes farinae mite culture has been undertaken by gel filtration. Two fractions were isolated. One, P25, is a protein-rich fraction with mol. wt about 25,000. The other, GP8, is a polysaccharide-rich fraction with mol. wt around 8,000. By crossed immunoelectrophoresis, we detected eleven antigens in the partially-purified dialysed D. farinae extract (Df 80d) as well as in P25 fraction. One of them, ag 11, seems the most important allergen since in crossed-radio immunoelectrophoresis experiments it displays the faster radiostaining, implying that it binds the greatest part of the mite-specific IgE present in a pool of sera from mite-sensitive patients. By crossed-line immunoelectrophoresis, we demonstrated the absence of ag 11 in GP8, in which only ag 5 and ag 6 were identifiable. By radioalloergosorbent tests (RAST), it was found that P25- and GP8- coated paper discs can fix specific IgE induced in the majority of D. farinae sensitive patients. Defining a 'major allergen' as an allergen to which the majority of sensitive patients develop specific IgE, both P25 and GP8 do appear to contain at least one major allergen. By RAST inhibition method, using Df 80d as a solid phase, the allergenic activity of P25 appeared as slightly higher than that of Df 80d, whereas GP8 displayed a very weak inhibitor capacity. Thus, the allergic specificity of GP8 differs from that of Df 80d or P25.