Glutathione conjugation of the fluorophotometric epoxide substrate, 7- glycidoxycoumarin (GOC), by rat liver glutathione transferase isoenzymes

1989 ◽  
Vol 38 (16) ◽  
pp. 2609-2613 ◽  
Author(s):  
Akira Hiratsuka ◽  
Akihiro Yokoi ◽  
Noriyuki Sebata ◽  
Tadashi Watabe ◽  
kimihiko Satoh ◽  
...  
Keyword(s):  
Rat Liver ◽  
Glutathione Transferase ◽  
Liver Glutathione ◽  
Glutathione Conjugation

scholarly journals Stereoselectivity of rat liver glutathione transferase isoenzymes for α-bromoisovaleric acid and α-bromoisovalerylurea enantiomers

1988 ◽  
Vol 252 (1) ◽  
pp. 137-142 ◽  
Author(s):  
J M Te Koppele ◽  
B Coles ◽  
B Ketterer ◽  
G J Mulder
Keyword(s):  
Catalytic Activity ◽  
Rat Liver ◽  
Multigene Family ◽  
Glutathione Transferase ◽  
Rat Hepatocytes ◽  
Isolated Rat Hepatocytes ◽  
Liver Glutathione ◽  
Amide Derivative ◽  
Isolated Rat

The stereoselectivity of purified rat GSH transferases towards alpha-bromoisovaleric acid (BI) and its amide derivative alpha-bromoisovalerylurea (BIU) was investigated. GSH transferase 2-2 was the only enzyme to catalyse the conjugation of BI and was selective for the (S)-enantiomer. The conjugation of (R)- and (S)-BIU was catalysed by the isoenzymes 2-2, 3-3 and 4-4. Transferase 1-1 was less active, and no catalytic activity was observed with transferase 7-7. Isoenzymes 1-1 and 2-2 of the Alpha multigene family preferentially catalysed the conjugation of the (S)-enantiomer of BIU (and BI), whereas isoenzymes 3-3 and 4-4 of the Mu multigene family preferred (R)-BIU. The opposite stereoselectivity of conjugation of BI and BIU previously observed in isolated rat hepatocytes and the summation of activities of enzymes known to be present in hepatocytes on the basis of present data are in accord.

scholarly journals Enzyme-catalysed reactions between some 2-substituted 5-nitrofuran derivatives and glutathione

1970 ◽  
Vol 119 (3) ◽  
pp. 463-472 ◽  
Author(s):  
E. Boyland ◽  
B. E. Speyer
Keyword(s):  
Nitro Group ◽  
Rat Liver ◽  
Human Liver ◽  
Glutathione Transferase ◽  
Liver Glutathione ◽  
Ph Values ◽  
Enzymic Reaction ◽  
Optimum Ph ◽  
Nitrofuran Derivatives

1. A glutathione transferase present in rat and human liver supernatant catalyses the reaction of some 2-substituted 5-nitrofuran derivatives with GSH, with formation of a conjugate and release of the nitro group as inorganic nitrite. Some of the substrates undergo the same reaction at a slower rate in the absence of enzyme. Nitrofuran derivatives commonly used as drugs, and five other drugs containing nitro groups, did not react. 2. Substrate activity in the nitrofuran derivatives showed an approximate correlation with the lability of the nitro group to alkali. 3. Optimum pH values ranging from 6.6 to 9.0 were found for the enzymic reaction with various derivatives, the values being influenced by alkali-lability and pK values of the compounds. 4. Tenfold purification of rat liver glutathione S-aryl-transferase resulted in an equal purification of the activities that catalyse the reaction of two of the nitrofuran derivatives with GSH.

Induction of rat liver glutathione transferase subunit 7 by lead nitrate

1989 ◽  
Vol 46 (3) ◽  
pp. 167-171 ◽  
Author(s):  
C. Di Ilio ◽  
A. Aceto ◽  
A. Columbano ◽  
G.M. Ledda-Columbano ◽  
G. Federici
Keyword(s):  
Rat Liver ◽  
Glutathione Transferase ◽  
Lead Nitrate ◽  
Liver Glutathione
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