Moneo Ignacio, Caballero Maria Luisa, González-Muñoz Miguel, Rodríguez-Mahillo Ana I, Rodríguez-Perez Rosa, Silva Augusto
Department of Immunology, Hospital Carlos III, Sinesio Delgado 10, 28029 Madrid, Spain.
Parasitol Res. 2005 Jul;96(5):285-9. doi: 10.1007/s00436-005-1362-2. Epub 2005 May 14.
The thermal stability of allergenic peptides from the fish parasite Anisakis simplex has not been fully elucidated. This is of special relevance for physicians who should clearly indicate if sensitized patients should avoid ingestion of raw fish only or whether well-cooked fish should also be avoided, if allergenic peptides derived from the parasite remain immunologically detectable. An allergen was purified after heating a crude parasite extract for 30 min. The allergen was further purified by an ethanol fractionation procedure followed by a reversed-phase HPLC. The N-terminal amino acid sequence was obtained. This allergen was detected by 27% of sensitized subjects. The N-terminal amino acid sequence of the 9 kDa allergen showed no similarities to other known proteins. A minor low molecular weight allergen from A. simplex is highly resistant to heating and it could therefore have significant clinical relevance.
鱼类寄生虫简单异尖线虫变应原性肽的热稳定性尚未完全阐明。这对医生而言具有特殊意义,因为如果致敏患者应避免仅食用生鱼,还是也应避免食用烹饪熟透的鱼(前提是源自该寄生虫的变应原性肽在免疫方面仍可检测到),医生需要明确指出。将粗制寄生虫提取物加热30分钟后,一种变应原得到了纯化。该变应原通过乙醇分级分离程序进一步纯化,随后进行反相高效液相色谱法分离。获得了其N端氨基酸序列。27%的致敏受试者检测到了这种变应原。9 kDa变应原的N端氨基酸序列与其他已知蛋白质无相似性。简单异尖线虫一种低分子量的次要变应原对加热具有高度抗性,因此可能具有重大临床意义。