Christie J F, Dunbar B, Davidson I, Kennedy M W
Wellcome Laboratories for Experimental Parasitology, University of Glasgow, U.K.
Immunology. 1990 Apr;69(4):596-602.
A protein allergen of the parasitic nematode Ascaris has been purified to homogeneity by immunoaffinity chromatography. It is the most abundant protein species in the parasite's body fluid and has been named ABA-1. The allergen's molecular weight (MW) has been previously estimated at 14,000, but this sizing is currently under re-evaluation. The immunological activity of the protein was intact after purification, as attested by immunoprecipitation and passive cutaneous anaphylaxis. The IgE response to ABA-1 was under major histocompatibility complex (MHC) restriction in the rat, in which only RT1u strains were found to respond following infection with the parasite. The tissue-invasive and intestinal stages of both Ascaris lumbricoides (of humans) and Ascaris suum (of pigs) have an antigen of similar MW to ABA-1 in their secretions or among their somatic antigens. These are antigenically indistinguishable; they were found to have similar amino acid compositions, and their N-terminal amino acid sequences were identical to 41 residues. Finally, the apparent MW, amino acid composition and isoelectric point of ABA-1 all argue for close similarity to the previously described Allergen A of the parasite.
一种寄生线虫蛔虫的蛋白质过敏原已通过免疫亲和层析纯化至同质。它是寄生物体液中含量最丰富的蛋白质种类，被命名为ABA - 1。该过敏原的分子量（MW）先前估计为14,000，但目前这一大小正在重新评估。纯化后该蛋白质的免疫活性保持完整，免疫沉淀和被动皮肤过敏反应证明了这一点。在大鼠中，对ABA - 1的IgE反应受主要组织相容性复合体（MHC）限制，其中只有RT1u品系在感染该寄生虫后被发现有反应。人蛔虫和猪蛔虫的组织侵袭期和肠道期在其分泌物或体抗原中都有一种与ABA - 1分子量相似的抗原。这些抗原在抗原性上无法区分；它们被发现具有相似的氨基酸组成，并且它们的N端氨基酸序列在41个残基处相同。最后，ABA - 1的表观分子量、氨基酸组成和等电点都表明它与该寄生虫先前描述的过敏原A非常相似。
