Purification and characterization of three distinct glutathione transferases from mouse liver

Biochemistry ◽  
1986 ◽  
Vol 25 (14) ◽  
pp. 4119-4125 ◽  
Author(s):  
Margareta Warholm ◽  
Helgi Jensson ◽  
Mohammad Kalim Tahir ◽  
Bengt Mannervik
1987 ◽  
Vol 25 (1-2) ◽  
pp. 111-121 ◽  
Author(s):  
Douglas K. Rex ◽  
William F. Bosron ◽  
Francis Dwulet ◽  
Ting-Kai Li

1989 ◽  
Vol 263 (2) ◽  
pp. 393-402 ◽  
Author(s):  
L I McLellan ◽  
J D Hayes

A novel cytosolic Alpha class glutathione S-transferase (GST) that is not normally expressed in mouse liver was found to be markedly induced (at least 20-fold) by the anti-carcinogenic compound butylated hydroxyanisole. This enzyme (designated GST Ya1 Ya1) did not bind to either the S-hexylglutathione-Sepharose or the glutathione-Sepharose affinity matrices, and purification was achieved by using bromosulphophthalein-glutathione-Sepharose. The purified isoenzyme, which comprises subunits of Mr 25,600, was characterized, and its catalytic, electrophoretic, immunochemical and structural properties are documented. GST Ya1 Ya1 was shown to be distinct from the Alpha class GST that is expressed in normal mouse liver and is composed of 25,800-Mr subunits; the Alpha class isoenzyme that is constitutively expressed in the liver is now designated GST Ya3 Ya3. Hepatic concentrations of GST Ya3 Ya3 were not significantly affected when mice were treated with butylated hydroxyanisole. Both Pi class GST (subunit Mr 24,800) and Mu class GST (subunit Mr 26,400) from female mouse liver were induced by dietary butylated hydroxyanisole. By contrast, hepatic concentrations of microsomal GST (subunit Mr 17,300) were unaffected.


2000 ◽  
Vol 275 (5) ◽  
pp. 3462-3468 ◽  
Author(s):  
Motohiro Tani ◽  
Nozomu Okino ◽  
Susumu Mitsutake ◽  
Tetsuo Tanigawa ◽  
Hiroyuki Izu ◽  
...  

1996 ◽  
Vol 52 (6) ◽  
pp. 901-910 ◽  
Author(s):  
Mahesh C. Sharma ◽  
Meena R. Sharma ◽  
Seong-Joo Jeong ◽  
Bernard H. Shapiro

Sign in / Sign up

Export Citation Format

Share Document