GLUTATHIONE S-TRANSFERASES IN EARTHWORMS (LUMBRICIDAE)

被引:44
作者
STENERSEN, J [1 ]
GUTHENBERG, C [1 ]
MANNERVIK, B [1 ]
机构
[1] UNIV STOCKHOLM,ARRHENIUS LAB,DEPT BIOCHEM,S-10691 STOCKHOLM,SWEDEN
关键词
D O I
10.1042/bj1810047
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:47 / 50
页数:4
相关论文
共 22 条
[1]   PURIFICATION AND CHARACTERIZATION OF 2 GLUTATHIONE S-ARYLTRANSFERASE ACTIVITIES FROM RAT-LIVER [J].
ASKELOF, P ;
GUTHENBERG, C ;
JAKOBSON, I ;
MANNERVIK, B .
BIOCHEMICAL JOURNAL, 1975, 147 (03) :513-522
[2]  
BEND J R, 1973, Bulletin of the Mount Desert Island Biological Laboratory, V13, P4
[3]   AN ENZYME FROM RAT LIVER CATALYSING CONJUGATIONS WITH GLUTATHIONE [J].
BOOTH, J ;
BOYLAND, E ;
SIMS, P .
BIOCHEMICAL JOURNAL, 1961, 79 (03) :516-&
[4]  
Clark A G, 1975, Environ Qual Saf Suppl, V3, P346
[5]   SPECIES DIFFERENCES IN INHIBITION OF GLUTATHIONE S-ARYLTRANSFERASE BY PHTHALEINS AND DICARBOXYLIC ACIDS [J].
CLARK, AG ;
DARBY, FJ ;
SMITH, JN .
BIOCHEMICAL JOURNAL, 1967, 103 (01) :49-&
[6]   METABOLISM OF GAMMEXANE IN FLIES TICKS AND LOCUSTS [J].
CLARK, AG ;
HITCHCOC.M ;
SMITH, JN .
NATURE, 1966, 209 (5018) :103-&
[7]   CROSS SPECIFICITY IN SOME VERTEBRATE AND INSECT GLUTATHIONE-TRANSFERASES WITH METHYL PARATHION (DIMETHYL P-NITROPHENYL PHOSPHOROTHIONATE), 1-CHLORO-2,4-DINITROBENZENE AND S-CROTONYL-N-ACETYLCYSTEAMINE AS SUBSTRATES [J].
CLARK, AG ;
SMITH, JN ;
SPEIR, TW .
BIOCHEMICAL JOURNAL, 1973, 135 (03) :385-392
[8]   DIRECT ENZYMIC METHOD FOR DETERMINATION OF REDUCED GLUTATHIONE IN BLOOD AND OTHER TISSUES [J].
CROWLEY, C ;
GILLHAM, B ;
THORN, MB .
BIOCHEMICAL MEDICINE, 1975, 13 (03) :287-292
[9]   TISSUE SULFHYDRYL GROUPS [J].
ELLMAN, GL .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1959, 82 (01) :70-77
[10]  
FJELLSTEDT TA, 1973, J BIOL CHEM, V248, P3702