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Plant and Cell Physiology, 2000, Vol. 41, No. 11 1293-1298
© 2000 Oxford University Press

Cloning and Functional Expression in Escherichia coli of a cDNA Encoding Cardenolide 16'-O-Glucohydrolase from Digitalis lanata Ehrh.

Johann J. Framm1, Angela Peterson2, Carola Thoeringer1, Antje Pangert1, Ellen Hornung3, Ivo Feussner3, Martin Luckner1,2,4 and Peter Lindemann1

1 Institut für Pharmazeutische Biologie, Martin-Luther-Universität, Hoher Weg 8, D-06120 Halle (Saale), Germany 2 Biozentrum, Weinbergweg 22, D-06120 Halle (Saale), Germany 3 Institut für Pflanzengenetik und Kulturpflanzenforschung, Corrensstrasse 3, D-06466 Gatersleben, Germany

A clone of cardenolide 16'-O-glucohydrolase cDNA (CGH I) was obtained from Digitalis lanata which encodes a protein of 642 amino acids (calculated molecular mass 73.2 kDa). The amino acid sequence derived from CGH I showed high homology to a widely distributed family of ß-glucohydrolases (glycosyl hydrolases family 1). The recombinant CGH I protein produced in Escherichia coli had CGH I activity. CGH I mRNA was detected in leaves, flowers, stems and fruits of D. lanata.

4 Corresponding author: E-mail, luckner@pharmazie.uni-halle.de; Fax, +49-345-5527213.


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