CAJ | 학술논문

目的：了解菲律宾蛤仔中过敏原的情况,对其主要过敏原进行鉴定和分子克隆。方法采用聚丙烯酰胺凝胶电泳和免疫印迹验证原肌球蛋白,双向电泳对蛋白等电点进一步确定。利用差示扫描量热法对蛋白的热性能测定以及蛋白克隆和测序来分析原肌球蛋白。结果菲律宾蛤仔原肌球蛋白的分子量在37 kDa左右,等电点为5.1,热稳定性较强。原肌球蛋白的基因序列全长为855 bp,编码284个氨基酸,对序列进行同源对比,相似性较高。结论本实验证实了原肌球蛋白为菲律宾蛤仔的过敏原,为认识菲律宾蛤仔过敏原提供基础数据。
목적：료해비률빈합자중과민원적정황,대기주요과민원진행감정화분자극륭。방법채용취병희선알응효전영화면역인적험증원기구단백,쌍향전영대단백등전점진일보학정。이용차시소묘량열법대단백적열성능측정이급단백극륭화측서래분석원기구단백。결과비률빈합자원기구단백적분자량재37 kDa좌우,등전점위5.1,열은정성교강。원기구단백적기인서렬전장위855 bp,편마284개안기산,대서렬진행동원대비,상사성교고。결론본실험증실료원기구단백위비률빈합자적과민원,위인식비률빈합자과민원제공기출수거。
ABSTRACT:Objective To investigate theRuditapes philippinarum allergen, and identify and clone the main allergens.MethodsTropomyosin was identified by polyacrylamide gel electrophoresis and immunoblotting, and isoelectric point was further analyzed by two dimensional electrophoresis. Thermal stability analysis was determined by differential scanning calorimetry, and tropomyosin was analyzed by cloning and sequencing of proteins. ResultsThe major allergen protein tropomyosin with the molecular weight 37 kDa was extracted. The isoelectric point was 5.1. Thetropomyosin ofR.philippinarumwas stable in the process of thermal treatment. The full-length cDNAs encoding tropomyosin was composed of 855 bp coding for 284 amino acid residues. The similarity of sequence was high through homologous comparison. ConclusionThe tropomyosin is the allergen of R.philippinarum. This research is helpful to provide the basic date to understandR.philippinarumallergen.