Primary sequence and site-selective hydroxylation of prolines in isoforms of a major peanut allergen protein Ara h 2
Primary sequence and site-selective hydroxylation of prolines in isoforms of a major peanut allergen protein Ara h 2
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DOI：
10.1002/pro.295
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发表时间：
2010-01-01
期刊：
影响因子：
8
通讯作者：
Fenselau, Catherine
中科院分区：
文献类型：
--
作者：
Li, Jinxi;Shefcheck, Kevin;Fenselau, Catherine
Ara h 2蛋白是花生过敏原的主要决定因素。这些蛋白质尚未在分子水平上得到充分研究。以前已经提出，有两个异构体的Ara h 2的基础上，推导出从两个报告的cDNA序列的一级结构。在这份报告中，四个异构体已被纯化，并分别进行了表征。质谱方法已被用来确定蛋白质序列，并确定所有四种亚型的翻译后修饰。已经鉴定了两对同种型，对应于长链形式和短12个氨基酸的形式。每一对通过蛋白质羧基末端是否存在两个氨基酸序列来进一步区分。修饰，其特征在于包括位点特异性羟基化的脯氨酸残基，但没有糖基化被发现，在以前的报告相反。
The Ara h 2 proteins are major determinants of peanut allergens. These proteins have not been fully studied at the molecular level. It has been previously proposed that there are two isoforms of Ara h 2, based on primary structures that were deduced from two reported cDNA sequences. In this report, four isoforms have been purified and characterized individually. Mass spectrometric methods have been used to determine the protein sequences and to define post-translational modifications for all four isoforms. Two pairs of isoforms have been identified, corresponding to a long-chain form and a form that is shorter by 12 amino acids. Each pair is further differentiated by the presence or absence of a two amino acid sequence at the carboxyl terminus of the protein. Modifications that were characterized include site-specific hydroxylation of proline residues, but no glycosylation was found, in contrast to previous reports.