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Two Apoplastic α-Amylases Are Induced in Tobacco by Virus Infection

Thierry Heitz, Pierrette Geoffroy, Bernard Fritig and Michel Legrand
Plant Physiology
Vol. 97, No. 2 (Oct., 1991), pp. 651-656
Stable URL: http://www.jstor.org/stable/4273884
Page Count: 6
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Two Apoplastic α-Amylases Are Induced in Tobacco by Virus Infection
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Abstract

α-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 α-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 extracellular localization was demonstrated by comparing the α-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 α-amylases produced in tobacco upon TMV infection.

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