为了在基因和蛋白表达水平上研究小麦的慢条锈性机制,运用双向电泳技术分析了条锈菌侵染的2个小麦品种(川麦107和80—8)的对照和发病14d叶片的差异表达蛋白,从2-D图谱上找到9个差异表达蛋白,其中点P5是在接种并发病的川麦107中新诱导出的一个差异蛋白质。通过基质辅助激光解析电离飞行时间质谱技术(MALDI—TOF—MS)获得6个蛋白质的肽指纹图谱(PMF),数据库搜索鉴定出2个蛋白质。这2个蛋白质是磷酸核酮糖激酶( Phosphoribulokinase, PRK)和脱氢抗坏血酸还原酶(Dehydroascorbate reductase,DHAR)
The changes of proteins in two wheat varieties, Chuanmail07and 80 - 8, caused by the inoculation of Puccina striiformis f. sp. tritici were analyzed using 2-dimentional electrophoresitic tech- nology. 9 protein spots resolved on 2-D gels were found to be differentially expressed after analyzing Coomas-blue stained gel of the soluble protein samples from the control and disease-affected leaves at 14 days post inoculation. These spots were then excised from gel and analysed by matrix-assisted laser desorption ionisation time of flight mass spectrometry (MALDI-TOF-MS). Peptide mass fingerprinting (PMF) of 6 proteins were submitted to NCBI and Swiss-prot databases for protein identification. Protein spot P5 only induced in Chuanmai 107 inoculated by CY32 was an unknown protein. 2 proteins identified were respectively phosphoribulokinase (PRK) and dehydroascorbate .reductase (DHAR). Proteome analysis of slow-rusting variety , Chuanmai 107, may provide clues for elucidating the resistant mechanisms of slow-rusting variety.