Journal Article

Cloning and Functional Expression in <i>Escherichia coli</i> of a cDNA Encoding Cardenolide 16′-<i>O</i>-Glucohydrolase from <i>Digitalis lanata</i> Ehrh.

Johann J. Framm, Angela Peterson, Carola Thoeringer, Antje Pangert, Ellen Hornung, Ivo Feussner, Martin Luckner and Peter Lindemann

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 41, issue 11, pages 1293-1298
Published in print November 2000 | ISSN: 0032-0781
Published online November 2000 | e-ISSN: 1471-9053 | DOI: http://dx.doi.org/10.1093/pcp/pcd060
Cloning and Functional Expression in Escherichia coli of a cDNA Encoding Cardenolide 16′-O-Glucohydrolase from Digitalis lanata Ehrh.

More Like This

Show all results sharing these subjects:

  • Biochemistry
  • Molecular and Cell Biology
  • Plant Sciences and Forestry

GO

Show Summary Details

Preview

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 β-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.

Keywords: Key words: Digitalis lanata — Glucosyl hydrolase (EC 3.2.1.21) — Lanatoside — Scrophulariaceae.; Abbreviations: CGH I, cardenolide 16′-O-glucohydrolase; CGH I, full length cDNA clone encoding for an isoenzyme of CGH I; IPTG, isopropyl β-d-thiogalactopyranoside.

Journal Article.  4042 words.  Illustrated.

Subjects: Biochemistry ; Molecular and Cell Biology ; Plant Sciences and Forestry

Full text: subscription required

How to subscribe Recommend to my Librarian

Users without a subscription are not able to see the full content. Please, subscribe or login to access all content.