花生主要过敏原Ara h 3的纯化、结晶及初步晶体学表征
Purification, crystallization and initial crystallographic characterization of peanut major allergen Ara h 3.
作者信息
Jin Tengchuan, Howard Andrew, Zhang Yu-Zhu
机构信息
Department of Biology, Illinois Institute of Technology, Chicago, IL 60616, USA.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Oct 1;63(Pt 10):848-51. doi: 10.1107/S1744309107041176. Epub 2007 Sep 19.
Abstract
The peanut is a significant food source, but is responsible for many cases of anaphylaxis. The peanut 11S legumin-like seed storage protein Ara h 3 is one of the best characterized allergens. In this study, Ara h 3 was extracted from peanut kernels and purified by sequential anion-exchange, hydrophobic interaction and gel-filtration chromatography to very high purity to facilitate crystallization and structural studies. Well diffracting single crystals were obtained by the vapor-diffusion method. A molecular-replacement structural solution has been obtained and refinement of the structure is currently under way.
摘要
花生是一种重要的食物来源，但会引发许多过敏反应病例。花生11S类豆球蛋白种子贮藏蛋白Ara h 3是特征最明确的过敏原之一。在本研究中，从花生仁中提取Ara h 3，并通过连续的阴离子交换、疏水相互作用和凝胶过滤色谱法将其纯化至非常高的纯度，以利于结晶和结构研究。通过气相扩散法获得了衍射良好的单晶。已获得分子置换结构解析，目前正在对结构进行精修。
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