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PMID: 486159 Published · ppublish English Comparative Study Journal Article

Glutathione S-transferases in earthworms (Lumbricidae).

The Biochemical journal ·Vol. 181 ·No. 1 ·1979-07-01 ·Pages 47-50

Stenersen J, Guthenberg C, Mannervik B

Abstract

Glutathione S-transferase activity (EC 2.5.1.18) was demonstrated in six species of earthworms of the family Lumbricidae: Eisenia foetida, Lumbricus terrestris, Lumbricus rebellus, Allolobophora longa, Allolobophora caliginosa and Allolobophora chlorotica. Considerable activity was obtained with 1-chlorl-2,4-dinitrobenzene and low activity with 3,4-dichloro-1-nitrobenzene, but no enzymic reaction was detectable with sulphobromophthalein 1,2-epoxy-3-(p-nitrophenoxy)propane of trans-4-phenylbut-3-en-2-one as substrates. Enzyme prepartations from L. rubellus and A. longa were the most active, whereas A. chlorotica gave the lowest activity. The ratio of the activities obtained with 1-chloro-2,4-dinitrobenzene and 3,4-cichloro-1-nitrobenzene was very different in the various species, but no phylogenetic pattern was evident. Isoelectric focusing gave rise to various activity peaks as measured with 1-chloro-2,4-dinitrobenzene as a substrate, and the activity profiles of the species examined appeared to follow a taxonomic pattern. The activity of Allolobophora had the highest peak in the alkaline region, whereas that of Lumbricus had the highest peak in the acid region. Eisenia showed a very complex activity profile, with the highest peak ne pH 7. As determined by an enzymic assay, all the species contained glutathione, on an average about 0.5 mumol/g wet wt. Conjugation with glutathione catalysed by glutathione S-transferases may consequently be an important detoxification mechanism in earthworms.

MeSH Terms
Animals Glutathione/analysis Glutathione Transferase/metabolism Isoelectric Focusing Oligochaeta/analysis,enzymology Species Specificity
Chemicals
Glutathione Transferase Glutathione
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Stenersen J
Guthenberg C
Mannervik B
References (16)
16 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
Published
1979-07-01
Pages
47-50
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1161123
Subset
IM
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