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作 者:高冬丽[1] 高金锋[1] 党根友[1] 冯佰利[1] 柴岩[1]
机构地区:[1]西北农林科技大学农学院,陕西杨凌712100
出 处:《华北农学报》2008年第2期68-71,共4页Acta Agriculturae Boreali-Sinica
基 金:科技部科技支撑计划(2006BAD02B06);教育部西部地区特色植物种质资源数据平台建设项目;陕西省科技攻关项目(2006K01-G17-01);西北农林科技大学育种专项资助
摘 要:采用十二烷基硫酸钠-聚丙烯酰胺凝胶电泳(SDS-PAGE)方法研究了荞麦的2个栽培种苦荞与甜荞的总蛋白、清蛋白、球蛋白及谷蛋白特性。试验结果表明,甜荞籽粒总蛋白及蛋白质各组分的谱带具有丰富的多态性,而苦荞籽粒总蛋白及蛋白质各组分谱带的多态性有限;荞麦清蛋白主要由低分子量的亚基构成;甜荞球蛋白组分包含由中等到低分子量范围的5-12种亚基,苦荞球蛋白主要由8种亚基组成;甜荞谷蛋白主要由分子量在43-66.2 kDa之间的3-5种亚基组成,苦荞谷蛋白主要由分子量在31-43 kDa间的2种亚基组成。Buckwheat( Fagopyrum esculentum Moench)proteins are nutritionally important because of their high and balanced content of essential amino acids making their biological value much higher than that of cereal proteins. In this paper, the subunits composition of albumin, globulin, and glutelin of common and tartary buckwheat, two cultured species, were determined using SDS-PAGE method, whose application has been found in many kinds of major crops. The results showed that high polymorphism was revealed among different common buckwheat cultivars while that among tartary buck- wheat was limited. The albumin of buckwheat was composed of subunits with low molecular weight. Common buckwheat globulin was composed of 5 - 12 subunits from low to middle molecular weight whereas only 8 subunits constituted tartary buckwheat globulin. Common buckwheat glutelin was composed of 3 - 5 subunits with molecular weight ranging within 43 - 66.2 kDa. Tartary buckwheat glutelin was composed of 2 subunits whose molecular weight ranged within 31 - 43 kDa.
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