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
-
An enzyme from rat liver catalysing conjugations with glutathione.
Biochem J. 1961 Jun;79(3):516-24
PMID: 16748905
-
Tissue sulfhydryl groups.
Arch Biochem Biophys. 1959 May;82(1):70-7
PMID: 13650640
-
The identity of glutathione S-transferase B with ligandin, a major binding protein of liver.
Proc Natl Acad Sci U S A. 1974 Oct;71(10):3879-82
PMID: 4139704
-
Metabolism of gammexane in flies, ticks and locusts.
Nature. 1966 Jan 1;209(5018):103
PMID: 4162689
-
Purification and characterization of two glutathione S-aryltransferase activities from rat liver.
Biochem J. 1975 Jun;147(3):513-22
PMID: 810139
-
A direct enzymic method for the determination of reduced glutathione in blood and other tissues.
Biochem Med. 1975 Jul;13(3):287-92
PMID: 1203068
-
Enzymatic conjugation of epoxides with glutathione.
J Biol Chem. 1973 May 25;248(10):3702-7
PMID: 4634012
-
Glutathione S-transferases. The first enzymatic step in mercapturic acid formation.
J Biol Chem. 1974 Nov 25;249(22):7130-9
PMID: 4436300
-
Cross specificity in some vertebrate and insect glutathione-transferases with methyl parathion (dimethyl p-nitrophenyl phosphorothionate), 1-chloro-2,4-dinitro-benzene and s-crotonyl-N-acetylcysteamine as substrates.
Biochem J. 1973 Nov;135(3):385-92
PMID: 4772267
-
Conjugations with glutathione. Distribution of glutathione S-aryltransferase in vertebrate species.
Biochem J. 1964 Mar;90(3):603-6
PMID: 4953591
-
Ligandin: a hepatic protein which binds steroids, bilirubin, carcinogens and a number of exogenous organic anions.
Nature. 1971 Dec 24;234(5330):466-7
PMID: 4944188
-
Glutathione S-transferase AA from rat liver.
Arch Biochem Biophys. 1976 Aug;175(2):710-6
PMID: 958327
-
Species differences in the inhibition of glutathione S-aryltransferase by phthaleins and dicarboxylic acids.
Biochem J. 1967 Apr;103(1):49-54
PMID: 6033774
-
Nature of a soluble, glutathione-dependent enzyme system active in cleavage of methyl parathion to desmethyl parathion.
J Econ Entomol. 1966 Dec;59(6):1338-46
PMID: 5976103
-
Spectrophotometric assay of the liver enzyme that catalyzes sulfobromophthalein-glutathione conjugation.
J Lab Clin Med. 1966 May;67(5):863-72
PMID: 5946041
-
Studies on glutathione S-alkyltransferase of the rat.
Biochem J. 1966 Jan;98(1):44-56
PMID: 5938663