Heitz T, Geoffroy P, Fritig B, Legrand M
Institut de Biologie Moléculaire des Plantes du Centre National de la Recherche Scientifique, Université Louis Pasteur, 12 rue du Général Zimmer 67084 Strasbourg Cédex, France.
Plant Physiol. 1991 Oct;97(2):651-6. doi: 10.1104/pp.97.2.651.
alpha-Amylase activity (EC 3.2. 1.1) is greatly increased in leaves of tobacco (Nicotiana tabacum L. cv Samsun NN) infected with tobacco mosaic virus (TMV). The kinetics of enzyme induction during the hypersensitive reaction resemble those of other hydrolases known to be pathogenesis-related proteins of tobacco. Two alpha-amylases were purified from TMV-infected leaves and shown to have features in common with well-characterized pathogenesis-related proteins: they are acidic monomers that can be separated upon electrophoresis on basic native gels, and they are found in the apoplastic compartment of the cell. This extra-cellular localization was demonstrated by comparing the alpha-amylase partition between the intercellular wash fluid and the cell extract with that of proteins of known cellular compartmentalization. These data indicate an active secretion of both alpha-amylases produced in tobacco upon TMV infection.
感染烟草花叶病毒（TMV）的烟草（Nicotiana tabacum L. cv Samsun NN）叶片中，α-淀粉酶活性（EC 3.2.1.1）大幅增加。过敏反应期间酶诱导的动力学与已知为烟草病程相关蛋白的其他水解酶相似。从感染TMV的叶片中纯化出两种α-淀粉酶，结果表明它们具有与特征明确的病程相关蛋白相同的特性：它们是酸性单体，在碱性天然凝胶上电泳时可分离，并且存在于细胞的质外体区室中。通过比较细胞间冲洗液和细胞提取物之间的α-淀粉酶分配与已知细胞区室化蛋白质的分配，证实了这种细胞外定位。这些数据表明，烟草在感染TMV后产生的两种α-淀粉酶均有活跃的分泌。
