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      Purification and characterisation of a non-plant myrosinase from the cabbage aphid Brevicoryne brassicae (L.).

      Insect Biochemistry and Molecular Biology
      Animals, Aphids, enzymology, Brassica, Glycoside Hydrolases, chemistry, isolation & purification, metabolism, Hydrogen-Ion Concentration, Isoelectric Point, Molecular Weight, Rabbits

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          Abstract

          Plant myrosinases and glucosinolates constitute a defence system in cruciferous plants towards pests and diseases. We have purified for the first time a non-plant myrosinase from the cabbage aphid Brevicoryne brassicae (L.) to homogeneity. The protein was N-terminally blocked and protease (trypsin and lys c) degradation gave peptides of which five were sequenced. The protein is a dimer with subunits of mass 54 kDa+/-500 Da. Western blot analysis with an anti-aphid myrosinase antibody showed a strong cross reaction with a protein extract from the Brassica specialist, B. brassicae. The anti-aphid myrosinase antibody does not cross react with plant myrosinase neither does an anti-plant myrosinase antibody cross react with aphid myrosinase.

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