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Schröder, P. ; Wolf, A.E.*

Characterization of glutathione S-transferases in needles of Norway spruce trees from a forest decline stand.

Tree Physiol. 16, 503-508 (1996)

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Open Access Green as soon as Postprint is submitted to ZB.

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Glutathione S-transferases (GST) detoxify many electrophilic xenobiotics, including several volatile organic compounds and pesticides. The GST activity for the conjugation of several xenobiotic substances was isolated from needles of Norway spruce (Picea abies L. Karst.) trees from a forest decline stand in the northern alps. Trees that exhibited different degrees of damage were selected from several stands in an altitude profile. The GST activity toward 1-chloro-2,4-dinitrobenzene (CDNB) in crude protein extracts of needles showed a seasonal pattern with highest activity during summer. The GST activity exhibited a strong dependence on the altitude of the stand showing highest activities in trees growing in the valley and lowest activities in trees growing in the summit regions of the mountain. When cytosolic GST from needles of healthy and damaged trees was purified, trees of healthy appearance exhibited three distinct GST isozymes with activities for the conjugation of CDNB and 1,2-dichloro-4-nitrobenzene (DCNB), whereas severely defoliated trees exhibited four GSTs with additional activity for the conjugation of ethacrynic acid. The main GST isozymes catalyzing the conjugation of CDNB differed in molecular weight, isoelectric point and catalytic properties between damaged and healthy trees.

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Publication type Article: Journal article

Document type Scientific Article

Corresponding Author

Keywords detoxification; isozymes; picea abies; xenobiotics

ISSN (print) / ISBN 0829-318X

e-ISSN 1758-4469

Journal Tree Physiology

Quellenangaben Volume: 16, Issue: 5, Pages: 503-508

Publisher Oxford University Press

Non-patent literature Publications

Reviewing status Peer reviewed

Institute(s) Institute of Biochemical Plant Pathology (BIOP)