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从两份西藏青稞材料中分离克隆出4个B组醇溶蛋白基因(BH1-BH4),DNA测序结果表明:它们均包含完整的开放阅读框。推断的氨基酸序列与先前报道的大麦B组醇溶蛋白具有相同的蛋白质基本结构。系统分析表明:它们推断的氨基酸序列与栽培大麦中的B组醇溶蛋白具有较高的相关性,与野生大麦和山羊草属的醇溶谷蛋白相似性较低。并且,在4个基因BH1-BH4中,BH1与先前报道的B组醇溶蛋白基因有较低的序列相似性,因此我们对BH1基因进行了原核表达,含该基因的表达载体在大肠杆菌中表达出相对分子质量为28．15 kDa．并以包涵体形式存在的蛋白,进一步对其在青稞谷粒品质改良中的潜在价值进行了探讨。
Four B-gliadin genes (BH1-BH4) were isolated and cloned from two Tibetan barley materials. The results of DNA sequencing showed that they all contained complete open reading frame (ORF). The deduced amino acid sequence has the same basic protein structure as the previously reported Barley Group B gliadin. Phylogenetic analysis showed that the deduced amino acid sequences were highly correlated with Group B gliadin in cultivated barley and lower in similarity to prolamin in wild barley and Aegilops sinensis. Moreover, among the four genes, BH1-BH4, BH1 has lower sequence similarity with the previously reported group B gliadin gene, so we carried out prokaryotic expression of BH1 gene. The expression vector containing this gene is expressed in E. coli The relative molecular mass was 28.15 kDa. The protein in the form of inclusion bodies was further explored for its potential value in the quality improvement of barley grains.