Acetaldehyde Content and Oxidative Stress in the Deleterious Effects of Alcohol Drinking on Rat Uterine Horn

Table 6

Glutathione S-transferase activity (GST), glutathione reductase activity (GRed), and glutathione peroxidase activity (GPx) in uterine horn and liver tissue from rats receiving an ethanol containing liquid diet.

Group*	GST nmol conjugated; GSH/min/mg protein	GRed nmol oxidized; NADPH/min/mg protein	GPx nmol oxidized; NADPH/min/mg protein
Uterine horn
Control	19±1	107±10	201±2
EtOH	31±1^a	106±5^b	177±2^a
Liver
Control	148±6	143±6	677±32
EtOH	152±1^b	223±5^a	664±26^b

∗Glutathione S-transferase activity (GST) in uterine horn tissue and liver cytosol (3.6–3.9 mg protein/ml for uterine horn and 18.5–19.8 mg protein/mL for liver) was assayed as the thioether formation with CDNB and reading the absorbance at 412 nm. Glutathione reductase activity (GRed) in uterine horn tissue and liver cytosol (3.6–4.1 mg protein/mL for uterine horn and 18.2–19.5 mg protein/mL for liver) was determined by measuring the disappearance of NADPH at 340 nm. Glutathione peroxidase activity (GPx) in uterine horn tissue and liver cytosol (1.4–1.9 mg protein/mL for uterine horn and 8.9–11.2 mg protein/mL for liver) was analyzed in a reaction initiated by H₂O₂ and following the absorbance change at 340 nm. Each value is the mean ± S.D. from four separate samples (five animals each). See Section 2 for details.
^a𝑃<0.01 when compared to control.
^b𝑃>0.05 when compared to control.