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.
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页码:47 / 50
页数:4
相关论文
共 22 条
[11]   NATURE OF A SOLUBLE GLUTATHIONE-DEPENDENT ENZYME SYSTEM ACTIVE IN CLEAVAGE OF METHYL PARATHION TO DESMETHYL PARATHION [J].
FUKAMI, JI ;
SHISHIDO, T .
JOURNAL OF ECONOMIC ENTOMOLOGY, 1966, 59 (06) :1338-&
[12]  
GOLDSTEIN J, 1966, J LAB CLIN MED, V67, P863
[13]   CONJUGATIONS WITH GLUTATHIONE - DISTRIBUTION OF GLUTATHIONE S-ARYLTRANSFERASE IN VERTEBRATE SPECIES [J].
GROVER, PL ;
SIMS, P .
BIOCHEMICAL JOURNAL, 1964, 90 (03) :603-&
[14]   IDENTITY OF GLUTATHIONE S-TRANSFERASE-B WITH LIGANDIN, A MAJOR BINDING-PROTEIN OF LIVER [J].
HABIG, WH ;
PABST, MJ ;
FLEISCHNER, G ;
GATMAITAN, Z ;
ARIAS, IM ;
JAKOBY, WB .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1974, 71 (10) :3879-3882
[15]   GLUTATHIONE S-TRANSFERASE AA FROM RAT-LIVER [J].
HABIG, WH ;
PABST, MJ ;
JAKOBY, WB .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1976, 175 (02) :710-716
[16]  
HABIG WH, 1974, J BIOL CHEM, V249, P7130
[17]   STUDIES ON GLUTATHIONE S-ALKYLTRANSFERASE OF RAT [J].
JOHNSON, MK .
BIOCHEMICAL JOURNAL, 1966, 98 (01) :44-&
[18]  
KALCKAR HM, 1947, J BIOL CHEM, V167, P461
[19]   LIGANDIN - HEPATIC PROTEIN WHICH BINDS STEROIDS, BILIRUBIN, CARCINOGENS AND A NUMBER OF EXOGENOUS ORGANIC ANIONS [J].
LITWACK, G ;
KETTERER, B ;
ARIAS, IM .
NATURE, 1971, 234 (5330) :466-&
[20]   PURIFICATION AND PROPERTIES OF HOUSEFLY GLUTATHIONE S-TRANSFERASE [J].
MOTOYAMA, N ;
DAUTERMAN, WC .
INSECT BIOCHEMISTRY, 1977, 7 (04) :361-369