Journal
BIOCHEMICAL JOURNAL
Volume 412, Issue -, Pages 535-544Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BJ20071464
Keywords
Chondrus crispus; glutathione transferase (GST); Laminaria digitata; methyl jasmonate; phylogenetic classification; recombinant protein
Categories
Ask authors/readers for more resources
The GSTs (glutathione transferases) are involved in the detoxification of a wide variety of hydrophobic substrates. These enzymes have been found in virtually all types of organisms, including plants, animals, nematodes and bacteria. In the present study, we report the molecular and biochemical characterization of algal GSTs. Phylogenetic analysis showed that most of them were distinct from previously described GST classes, but were most closely related to the Sigma class. Profiling of GST genes from the red alga Chondrus crispus and brown alga Laminaria digitata was undertaken after different chemical treatments and showed that they displayed contrasting patterns of transcription. Recombinant algal GST from both species showed transferase activities against the common substrates aryl halides, but also on the alpha,beta-unsaturated carbonyl 4-hydroxynonenal. Also, they exhibit significant peroxidation towards organic hydroperoxides, including oxygenated derivatives of polyunsaturated fatty acids. Among a range of compounds tested, Cibacron Blue was the most efficient inhibitor of algal GSTs identified.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available