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Research article1995Peer reviewed

Characterization of rapeseed myrosinase-binding protein.

Falk A, Taipalensuu J, Ek B, Lenman M, Rask L

Abstract

Myrosinase-binding proteins (MBPs) were purified from seeds of Brassica napus L. (oilseed rape). The proteins were characterized with respect to amino-acid composition, peptide sequence and isoelectric points. Gel electrophoresis and Western blotting of protein extracts from mature seeds showed the existence of at least ten proteins reacting with a monoclonal anti-MBP antibody and ranging in molecular size from 110 to 30 kDa. Proteins other than MBP reacting with the anti-MBP antibody were assigned as myrosinase-binding protein-related proteins (MBPRPs). Two MBPRPs were purified by immunoaffinity chromatography and characterized with respect to partial amino-acid sequence. Sequence identities were found between MBP and MBPRP. Western blot analysis of protein extracts from different tissues of B. napus showed that MBPRP is present in the whole plant, whereas MBP mostly occurs in the mature seed. A double-antibody sandwich enzyme-linked immunosorbent assay (ELISA) was used to investigate the occurrence of MBP and MBPRP in developing seeds of some species in the Brassicaceae family.

Published in

Planta
1995, Volume: 195, number: 3, pages: 387-395

      SLU Authors

    • Falk, Anders

      • Department of Cell Research, Swedish University of Agricultural Sciences
      • Ek, Bo

        • Department of Cell Research, Swedish University of Agricultural Sciences
        • Lenman, Marit

          • Department of Cell Research, Swedish University of Agricultural Sciences
          • Rask, Lars

            • Department of Cell Research, Swedish University of Agricultural Sciences

          UKÄ Subject classification

          Agricultural Science

          Publication identifier

          DOI: https://doi.org/10.1007/BF00202596

          Permanent link to this page (URI)

          https://res.slu.se/id/publ/40470