Computational and Experimental Studies on the Distribution of Addition and Substitution Products of the Microsomal Glutathione Transferase 1-Catalyzed Conjugation of Glutathione with Fluoroalkenes

2003 ◽  
Vol 16 (2) ◽  
pp. 137-144 ◽  
Author(s):  
Larry J. Jolivette ◽  
M. W. Anders
1998 ◽  
Vol 123 (2) ◽  
pp. 87-96 ◽  
Author(s):  
Ingeborg Schmidt-Krey ◽  
Gerd Lundqvist ◽  
Ralf Morgenstern ◽  
Hans Hebert

1984 ◽  
Vol 33 (22) ◽  
pp. 3609-3614 ◽  
Author(s):  
Ralf Morgenstern ◽  
Gerd Lundqvist ◽  
Göran Andersson ◽  
Lennart Balk ◽  
Joseph W. Depierre

Biochemistry ◽  
2017 ◽  
Vol 56 (24) ◽  
pp. 3089-3098 ◽  
Author(s):  
Linda Spahiu ◽  
Johan Ålander ◽  
Astrid Ottosson-Wadlund ◽  
Richard Svensson ◽  
Carina Lehmer ◽  
...  

1988 ◽  
Vol 250 (3) ◽  
pp. 713-718 ◽  
Author(s):  
M Söderström ◽  
S Hammarström ◽  
B Mannervik

Leukotriene C4 synthesis was studied in preparations from mouse mastocytoma cells. Enzymic conjugation of leukotriene A4 with glutathione was catalysed by both the cytosol and the microsomal fraction. The specific activity of the microsomal fraction (7.8 nmol/min per mg of protein) was 17 times that of the cytosol fraction. The cytosol fraction of the mastocytoma cells contained two glutathione transferases, which were purified to homogeneity and characterized. A microsomal glutathione transferase was purified from mouse liver; this enzyme was shown by immunoblot analysis to be present in the mastocytoma microsomal fraction at a concentration one-tenth or less of that in the liver microsomal fraction. Both the cytosolic and the microsomal glutathione transferases in the mastocytoma cells were identified with enzymes previously characterized, by determining specific activities with various substrates, sensitivities to inhibitors, reactions with antibodies, and physical properties. The purified microsomal glutathione transferase from liver was inactive with leukotriene A4 or its methyl ester as substrate. The cytosolic enzymes displayed activity with leukotriene A4, but their specific activities and intracellular concentrations were too low to account for the leukotriene C4 formation in the mastocytoma cells. The microsomal fraction of the cells contained an enzyme distinguishable by various criteria from the previously studied glutathione transferases. This membrane-bound enzyme, leukotriene C synthase (leukotriene A4:glutathione S-leukotrienyltransferase), appears to carry the main responsibility for the biosynthesis of leukotriene C4.


2011 ◽  
Vol 43 (2) ◽  
pp. 300-306 ◽  
Author(s):  
Ralf Morgenstern ◽  
Jie Zhang ◽  
Katarina Johansson

FEBS Letters ◽  
1993 ◽  
Vol 315 (1) ◽  
pp. 77-80 ◽  
Author(s):  
E. Mosialou ◽  
C. Andersson ◽  
G. Lundqvist ◽  
G. Andersson ◽  
T. Bergman ◽  
...  

Biochemistry ◽  
2000 ◽  
Vol 39 (49) ◽  
pp. 15144-15149 ◽  
Author(s):  
Richard Svensson ◽  
Rosanna Rinaldi ◽  
Stellan Swedmark ◽  
Ralf Morgenstern

2017 ◽  
Vol 73 ◽  
pp. 79-87 ◽  
Author(s):  
Zhen Zhang ◽  
Zhimeng Lv ◽  
Yina Shao ◽  
Qiongfen Qiu ◽  
Weiwei Zhang ◽  
...  

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