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Isolation and characterization of two acyl-CoA-binding proteins from proembryogenic masses of Digitalis lanata Ehrh.

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Abstract.

 Two acyl-CoA-binding-protein (ACBP) isoforms were isolated from proembryogenic masses of Digitalis lanata Ehrh. by column chromatography and preparative HPLC. The ACBPs had molecular masses of 9926 and 9997 Da, respectively. Partial sequence data indicated high similarity to each other and to ACBPs of other plant species such as Ricinus communis, Brassica napus and Arabidopsis thaliana. The isolated ACBPs bound palmitoyl-CoA with high affinity as determined by isoelectric-point shift.

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Authors and Affiliations

  1. Institut für Pharmazeutische Biologie, Martin-Luther-Universität Halle-Wittenberg, Hoher Weg 8, 06120 Halle/Saale, Germany, , , , , , DE

    Martin Metzner, Frieder Mueller-Uri & Beate Diettrich

  2. Max-Planck-Forschungstelle “Enzymologie der Proteinfaltung”, Weinbergweg 22, 06120 Halle/Saale, Germany, , , , , , DE

    Karl Peter Ruecknagel & Gerhard Kuellertz

  3. Institute of Biochemistry, Odense University, Campusvej 55, 5230 Odense, Denmark, , , , , , DK

    Jens Knudsen

Authors
  1. Martin Metzner
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  2. Karl Peter Ruecknagel
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  3. Jens Knudsen
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  4. Gerhard Kuellertz
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  5. Frieder Mueller-Uri
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  6. Beate Diettrich
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Received: 29 May 1999 / Accepted: 28 August 1999

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Metzner, M., Ruecknagel, K., Knudsen, J. et al. Isolation and characterization of two acyl-CoA-binding proteins from proembryogenic masses of Digitalis lanata Ehrh.. Planta 210, 683–685 (2000). https://doi.org/10.1007/s004250050060

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  • DOI: https://doi.org/10.1007/s004250050060

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