scholarly journals The purification of the hepatic glutathione S-transferases of rainbow trout by glutathione affinity chromatography alters their isoelectric behaviour

1983 ◽  
Vol 211 (2) ◽  
pp. 523-526 ◽  
Author(s):  
P I N Ramage ◽  
I A Nimmo
Keyword(s):  
Rainbow Trout ◽  
Affinity Chromatography ◽  
Reduced Glutathione ◽  
Affinity Column ◽  
High Ph ◽  
Hepatic Glutathione ◽  
Glutathione S Transferases ◽  
Glutathione Oxidation ◽  
Rainbow Trout Liver

1. The basic glutathione S-transferases from rainbow-trout liver were more stable than the acidic ones. 2. The apparent pI values of these enzymes were lowered when they were eluted from a glutathione affinity column by reduced glutathione at pH 8.85. 3. The pI effect was not a function of the high pH alone, was diminished under conditions less favourable to glutathione oxidation, and did not occur when S-hexylglutathione affinity chromatography was used instead.

scholarly journals Purification and characterization of hepatic glutathione S-transferases of rhesus monkeys. A family of enzymes similar to the human hepatic glutathione S-transferases

1988 ◽  
Vol 251 (1) ◽  
pp. 81-88 ◽  
Author(s):  
R M Hoesch ◽  
T D Boyer
Keyword(s):  
Peroxidase Activity ◽  
Rhesus Monkeys ◽  
Affinity Column ◽  
Terminal Sequence ◽  
Glutathione S Transferase ◽  
Substrate Specificities ◽  
High Affinity ◽  
Human Enzyme ◽  
Hepatic Glutathione ◽  
Glutathione S Transferases

Thirteen forms of glutathione S-transferase were purified from the livers of female rhesus monkeys (Macaque mulatta). Most (74.7%) of the activity in the hepatic cytosol adhered well to the GSH affinity column and could be eluted only with the addition of GSH to the eluting buffer. The predominant isoenzymes (n = 5) in this ‘high-affinity’ fraction had alkaline pI values (greater than 9.0) and contained a subunit with an Mr value of 24,000. All of these isoenzymes had high organic peroxidase activity and, on the basis of amino acid analysis, substrate specificities and affinity for non-substrate ligands, appear to belong to the family of glutathione S-transferases that have been termed alpha [Mannervik, Alin, Guthenberg, Jensson, Tahir, Warholm & Jörnvall (1985) Proc. Natl. Acad. Sci. U.S.A. 82, 7202-7206]. Also within the high-affinity fraction was an isoenzyme with an acidic (5.8) pI value. This acidic isoenzyme was composed of a unique subunit (Mr 23,000). The N-terminal sequence (ten residues) of this acidic enzyme was identical with that of a human form that is referred to as pi. The predominant form of enzyme in the ‘low-affinity’ (eluted from the GSH affinity column with an increase in buffer pH) fraction was a homodimer of a 26,000-Mr subunit. It had an alkaline pI (greater than 9.0) but it lacked organic peroxidase activity. The N-terminal sequence (ten residues) of this enzyme was identical with that of a human enzyme referred to as mu. The substrate specificities and affinity for non-substrate ligands of this monkey enzyme also were similar to those of the human enzyme. In conclusion, the liver cytosol of rhesus monkeys contains a number of glutathione S-transferase isoenzymes that are very similar to the human hepatic enzymes.

Affinity chromatography of hepatic glutathione S-transferases on ω-aminoalkyl sepharose derivatives of glutathione

1981 ◽  
Vol 659 (2) ◽  
pp. 362-369 ◽  
Author(s):  
Masayasu Inoue ◽  
Michiaki Hara ◽  
Fujio Nagashima ◽  
Sunao Matsui ◽  
Nobuo Mitsuyasu ◽  
...  
Keyword(s):  
Affinity Chromatography ◽  
Hepatic Glutathione ◽  
Glutathione S Transferases ◽  
Derivatives Of

Bergenin Exhibits Hepatoprotective Activity Against Ethanol-Induced Oxidative Stress in ICR Mice

2019 ◽  
Vol 18 (4) ◽  
pp. 297-302
Author(s):  
Sriset Yollada ◽  
Chatuphonprasert Waranya ◽  
Jarukamjorn Kanokwan
Keyword(s):  
Reactive Oxygen Species ◽  
Gallic Acid ◽  
Aspartate Aminotransferase ◽  
Alanine Aminotransferase ◽  
Hepatic Injury ◽  
Reduced Glutathione ◽  
Reactive Oxygen ◽  
Hepatoprotective Activity ◽  
Oxygen Species ◽  
Hepatic Glutathione

Bergenin is a C-glucoside derivative of gallic acid but its antioxidant and hepatoprotective effects have not previously been compared with gallic acid. Male ICR mice were administered bergenin (10, 50, and 250 mg/kg/day) or gallic acid (100 mg/kg/day) for 7 consecutive days before a single administration of ethanol (5 g/kg). Liver sections were histopathologically examined. Aspartate aminotransferase, alanine aminotransferase, reactive oxygen species, and malondialdehyde levels were determined in plasma. Total glutathione, reduced glutathione, and oxidized glutathione levels were determined in liver homogenates. Ethanol induced hepatic injury with prominent histopathological markers including nuclear pyknosis and necrotic areas and this accorded with increases in the plasma levels of aspartate aminotransferase, alanine aminotransferase, reactive oxygen species, and malondialdehyde. Moreover, ethanol disturbed hepatic glutathione homeostasis by reducing glutathione stores. Hepatic injury in the ethanol-induced mice was prevented with bergenin and gallic acid by significant decreases in plasma aspartate aminotransferase, alanine aminotransferase, reactive oxygen species, and malondialdehyde levels and restoration of the hepatic glutathione profile through an increase in the reduced glutathione/oxidized glutathione ratio. Bergenin at 10 mg/kg/day showed comparable hepatoprotective activity to gallic acid in an ethanol-induced mouse model of oxidative stress. Therefore, bergenin might be a promising candidate for further development as a novel hepatoprotective product.

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