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Superoxide anion scavenger properties of sparteine, a quinolizidine alkaloid from Lupinus
Peroxidase activity in lupin ( Lupinus albus cv. Multolupa) hypocotyls is located, as are quinolizidine-type alkaloids, in epidermal tissues. Since these alkaloids have been shown to suffer a rapid turnover and degradation in lupin tissues, the ability of sparteine (a typical tetracyclic quinolizidi...
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Published in: | Journal of plant physiology 1997, Vol.150 (1), p.5-8 |
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Main Authors: | , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | Peroxidase activity in lupin (
Lupinus albus cv. Multolupa) hypocotyls is located, as are quinolizidine-type alkaloids, in epidermal tissues. Since these alkaloids have been shown to suffer a rapid turnover and degradation in lupin tissues, the ability of sparteine (a typical tetracyclic quinolizidine alkaloid) and cytisine (a typical tricyclic α-pyridone quinolizidine alkaloid) to act as peroxidase substrates was studied. However, neither alkaloid was oxidized by a partially purified lupin peroxidase fraction, or by horseradish peroxidase, as was ascertained by spectrophotometric and GC-MS studies. Likewise, these quinolizidine-type alkaloids were not substrates of a laccase of fungal origin. However, sparteine, unlike cytisine, acted as a superoxide scavenger, when the superoxide anions were generated in a phenazin methosulphate-NADH system and determined by the superoxide dismutase-sensitive reduction of nitroblue tetrazolium. The IC
50 value was 2.0 mmol/L. These results are discussed in the light of a possible protective role against oxidative damage of sparteine in
Lupinus. |
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ISSN: | 0176-1617 1618-1328 |
DOI: | 10.1016/S0176-1617(97)80173-3 |