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Two Apoplastic α-Amylases Are Induced in Tobacco by Virus Infection
Thierry Heitz, Pierrette Geoffroy, Bernard Fritig and Michel Legrand
Vol. 97, No. 2 (Oct., 1991), pp. 651-656
Published by: American Society of Plant Biologists (ASPB)
Stable URL: http://www.jstor.org/stable/4273884
Page Count: 6
You can always find the topics here!Topics: Gels, Enzymes, Leaves, Plants, Starches, Peas, Electrophoresis, Cell extracts, pH, Sodium
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α-Amylase activity (EC 126.96.36.199) 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.
Plant Physiology © 1991 American Society of Plant Biologists (ASPB)