| 水稻纹枯病菌PG的分离纯化及其理化性质研究 |
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| 引用本文： | 陈夕军,王友德,左示敏,童蕴慧,潘学彪,徐敬友.水稻纹枯病菌PG的分离纯化及其理化性质研究[J].植物病理学报,2010,40(3):276-281. |
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| 作者姓名： | 陈夕军 王友德 左示敏 童蕴慧 潘学彪 徐敬友 |
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| 作者单位： | 1 扬州大学园艺与植物保护学院, 扬州 225009;2 扬州大学江苏省作物遗传生理重点实验室/植物功能基因组学教育部重点实验室, 扬州 225009 |
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| 基金项目： | 农业公益性行业专项，扬州大学校基金，扬州大学创新培育基金 |
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| 摘 要： | 水稻纹枯病菌产生的多聚半乳糖醛酸酶(Polygalacturonase,PG)是其重要的致病因子之一。用丙酮法提取PG粗蛋白,分别经DEAE-Sepharose Fast Flow离子交换柱、Phenyl-Sepharose 6 Fast Flow疏水柱、Sephadex G-75凝胶柱和DE52离子交换柱层析纯化得到一种具有较高活性的PG纯蛋白。该蛋白分子量为39.81 kD;等电点为4.58;含有糖基,含糖量为1.48%;含有α氨基酸,但不含芳香族氨基酸;不含脂基。这种蛋白在pH4~12范围内均具有活性,pH5时活性最大;对热不稳定,100℃下水浴20 min,活性完全丧失;对胰蛋白酶和蛋白酶K敏感,酶处理后其活性只有对照的35.0%和35.2%;对紫外线和氯仿亦敏感,处理后活性仅为对照的40.0%和51.7%。
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| 关 键 词： | 水稻纹枯病菌 PG蛋白 分离纯化 理化性质 |
Isolation,purification and characterization of polygalacturonase(PG)from Rhizoctonia solani,the pathogen of rice sheath blight |
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| CHEN Xi-jun,WANG You-de,ZUO Shi-min,TONG Yun-hui,PAN Xue-biao,XU Jing-you.Isolation,purification and characterization of polygalacturonase(PG)from Rhizoctonia solani,the pathogen of rice sheath blight[J].Acta Phytopathologica Sinica,2010,40(3):276-281. |
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| Authors: | CHEN Xi-jun WANG You-de ZUO Shi-min TONG Yun-hui PAN Xue-biao XU Jing-you |
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| Institution: | 1 Horticulture and Plant Protection College, Yangzhou University, Yangzhou 225009, China;2 Key Laboratory of Plant Functional Genomics of Ministry of Education/Key Laboratory of Crop Genetics and Physiology of Jiangsu Province, Yangzhou University, Yangzhou 225009, China |
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| Abstract: | Polygalacturonases produced from Rhizoctonia solani, the pathogen of rice sheath blight, was one of the most important pathogenitic factors. The crude protein of polygalacturonases in culture filtrate was precipitated with acetone and then purified by DEAE-Sepharose Fast Flow ion exchange column, Phenyl-Sepharose 6 Fast Flow hydrophobic column, Sephadex G-75 gel column and DE52 ion exchange column in turn. Molecular weight of the protein was 39.81 kD by DSD-PAGE and PI value was 4.58 by IEF-PAGE. The protein was demonstrated as glycoprotein that contained 1.48% saccharide and α-amino acid, but no proline or hydroxyproline and lipid. The activity of the protein was observed in the range of pH 4 to 12, and the strongest was at pH 5. The protein lost activity at 100℃ for 20 min, and was also sensitive to trypsin, proteinase K, ultraviolet radiation and chloroform. After being treated with above, the activity of the protein was only 35.0%, 35.2%, 40.0% and 51.7% of the contrast respectively. |
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| Keywords: | Rhizoctonia solani PG protein isolation and purification characteristics |
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