You are here:
| Reference : Differences in glucosinolate degradation products related to aphid and Brassicaceae host... |
| Scientific journals : Article | |||
| Life sciences : Entomology & pest control | |||
| http://hdl.handle.net/2268/24132 | |||
| Differences in glucosinolate degradation products related to aphid and Brassicaceae host plant myrosinases | |
| English | |
| Francis, Frédéric [Université de Liège - ULg > Gembloux Agro-Bio Tech > Gembloux Agro-Bio Tech >] | |
Wathelet, Jean-Paul  [Université de Liège - ULg > Gembloux Agro-Bio Tech > Gembloux Agro-Bio Tech >] | |
| Lognay, Georges [Université de Liège - ULg > Gembloux Agro-Bio Tech > Gembloux Agro-Bio Tech >] | |
| 2001 | |
| GCIRC Bulletin | |
| No | |
| International | |
| [en] glucosinolate ; myrosinase ; aphid | |
| [en] Studies on chemical ecology of host plant selection by herbivores were largely carried out to orplain
the diversity of secondary plant chemicals and host specialisation of herbivores. The glucosinolate - isothiocyanate system in Brassicaceae plants was considered as a plant defence and was known to influence the feeding behaviour of phytophagous insects such as the cabbage aphid, Brevicoryre brassicae. Purified m5nosinases from the latter and from white mustard, Sinqis alba, were used to hydrolyse two glucosinolate compounds. Identification of the degradation products, mainly isothiocyanates, was perficrmed by gas chromatography - mass spectromeûy. While sinigdn hydrolysis gave identical isothiocyanates for insect and plant enzymes, B. brassicae myrosinase showed a particular activity toward sinalbin A lost of an hydrory group was obsen'red for the two latter substrates related products when compared to the S. alba enzymatic specificity. Aphid and plant myrosinases have different properties and specificities which can be discussed in relation to a co-evolution approach. | |
| http://hdl.handle.net/2268/24132 |
| File(s) associated to this reference | ||||||||||||||
|
Fulltext file(s):
| ||||||||||||||
All documents in ORBi are protected by a user license.
