Partial purification and properties of the sesquiterpene β-selinene cyclase from Citrofortunella mitis fruits
Autor: | Ginette Pauly, L. Belingheri, Alain Cartayrade, M. Gleizes |
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Rok vydání: | 1992 |
Předmět: |
chemistry.chemical_classification
Chromatography Size-exclusion chromatography Ion chromatography Substrate (chemistry) Plant Science General Medicine Biology Sesquiterpene Cyclase chemistry.chemical_compound Isoelectric point Enzyme chemistry Biochemistry Genetics Selinene Agronomy and Crop Science |
Zdroj: | Plant Science. 84:129-136 |
ISSN: | 0168-9452 |
Popis: | From a supernatant fraction of the peripheral flavedo of immature calamondin ( Citrofortunella mitis ) fruits were extracted by sesquiterpene cyclase catalyzing the conversion of farnesyl diphosphate to β-selinene. This enzyme was partially purified by ion exchange chromatography and its properties were investigated. The molecular weight was estimated to be in the range of 67 000 by gel filtration. The K m for the substrate farnesyl diphosphate was found to be 45 μM. This protein exhibited an isoelectric point of 6.0. It required the presence of divalent metal cations and Mg 2+ was preferred to Mn 2+ . |
Databáze: | OpenAIRE |
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