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作 者:赵明治[1] 杨秀芬[2] 张明[1] 袁京京[2] 邱德文[2]
机构地区:[1]安徽农业大学生命科学学院,合肥230036 [2]中国农业科学院植物保护研究所,北京100081
出 处:《中国生物防治》2007年第2期170-173,共4页Chinese Journal of Biological Control
基 金:"973"项目(2003CB114204);北京市科技计划(D0706005040431)
摘 要:通过硫酸铵沉淀、有机溶剂沉淀、离子交换和分子筛连用的方法,从极细链格孢菌JH505菌株中分离纯化到分子量约为35kD的植物激发子。利用固相梯度凝胶双向电泳方法测定了该蛋白的等电点为4.22。将该纯化蛋白稀释液浸泡小麦种子8h,7d后小麦根系琥珀酸脱氢酶活性提高65.27%,经蛋白处理的小麦根长比对照提高13.1%。A new plant activator from Alternaria tenuissima was purified using ammonium sulphate frac- tionation, organic solvent, anion exchange chromatography and size exclusion chromatography. The protein exhibited a single band on SDS-PAGE with molecular weight of 35 kD. Its pI was determined as 4.22 using immobiline dry strip gel. The wheat seeds were treated with the purified elicitor at various concentrations for 8 h and the succinate dehydrogenase was measured after 7 d growth. The result showed that the protein has a remarkable effect on the activity of succinate dehydrogenase which was 65.27 % higher than that of control. Also, the length of main root was improved 13.1% comparing to the control.
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