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作 者:代寿芬[1] 颜泽洪[1] 魏育明[1] 郑有良[1]
机构地区:[1]四川农业大学小麦研究所,四川都江堰611830
出 处:《四川农业大学学报》2008年第1期1-4,共4页Journal of Sichuan Agricultural University
基 金:国家自然科学基金(30370882;30671272);教育部全国高等学校优秀博士论文作者专项基金(200458);四川省青年基金(04ZQ026-040);四川省教育厅科研项目
摘 要:为了认识节节麦5t+12t亚基品质表现突出的分子基础,利用SDS-PAGE分析研究了该亚基组合中12t亚基的电泳迁移率并克隆和测序了该亚基基因。结果表明,该12t亚基在SDS-PAGE上的电泳迁移率与普通小麦中的Dy12具有一致的电泳迁移率,但与Dy10的电泳迁移率差异明显。而氨基酸序列比较结果显示,12t亚基的分子序列与Dy10的相似程度非常高,二者仅存在4个氨基酸的替换,而它与Dy12的分子序列存在较大的差异,不但包括12个氨基酸的替换,同时包括2个六肽氨基酸和另外4个氨基酸部位的插入和缺失变化。本研究结果表明,节节麦高分子量谷蛋白Dx5t+Dy12t亚基赋予小麦优良加工品质的主要原因可能与12t亚基与小麦Dy10非常相似,导致这一亚基组合更倾向与Dx5+Dy10有一定关系。To understand the molecular bases for HMW glutenin subunit Dx5^t + Dy12^t endowing wheat flours with prominent end use qualities, the electrophoresis mobility of Dy12^t in this subunit combinations was determined by SDS - PAGE analysis and the gene for this subunit was isolated and sequenced. Results showed that the electrophoresis mobility of HMW glutenin Dy12^t of Aegilops tauschii and Dy12 of wheat are the same, while both are distinctively different from Dy10 of wheat. However, at amino acid sequence level, HMW glutenin Dy12^t differs from Dy10 only by four amino acid replacement, while they showed great difference with Dy12 by twelve amino acid replacements and two hexpeptide insertions and four amino acid insertions/deletions. The results suggested that the main reason for Ae. tauschii HMW glutenin Dx5^t + Dy12^t endowing wheat with good baking quality could ascribe to the high similarity between HMW glutenin Dy12^t and Dy10 at amino acid sequence level, which makes the quality potential of HMW glutenin subunit pair Dx5^t + Dy12^t is very like that of Dx5 + Dy10.
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