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Cloning and functional expression in Escherichia coli of a cDNA encoding cardenolide 16'-O-glucohydrolase from
J J Framm1, A Peterson, C Thoeringer
1Institut für Pharmazeutische Biologie, Martin-Luther-Universität, Hoher Weg 8, D-06120 Halle (Saale), Germany.
Plant & Cell Physiology
|November 28, 2000
Abstract:
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 beta-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.