Increased liver-specific catalase activity in transgenic mice

DNA and Cell Biology

Volumn 15, Issue 8, 1996, Pages 625-630

  Nilakantan, Vani ^a  

^a Dept of Nutrition and Food Science   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACYL COENZYME A DEHYDROGENASE; CATALASE; HYDROGEN PEROXIDE; LAURATE HYDROXYLASE; LAURIC ACID DERIVATIVE; PEROXISOME PROLIFERATOR; UNCLASSIFIED DRUG;

ANIMAL CELL; ANIMAL MODEL; ARTICLE; DETOXIFICATION; DNA DAMAGE; ENZYME ACTIVATION; ENZYME MECHANISM; ENZYME REGULATION; ENZYME SPECIFICITY; HUMAN; HUMAN CELL; MOUSE; NONHUMAN; PRIORITY JOURNAL; TRANSGENIC MOUSE; TUMOR PROMOTION;

EID: 0029785776     PISSN: 10445498     EISSN: None     Source Type: Journal    
DOI: 10.1089/dna.1996.15.625     Document Type: Article

References (4)

1. AMSTAD, P., PESKIN, A., SHAH, G., MIRAULT, M., MORET, R., ZBINDEN, I., and CERUTTI, P. (1991). The balance between Cu,Zn-superoxide dismutase and catalase affects the sensitivity of mouse epidermal cells to oxidative stress. Biochemistry 30, 9305-9313.
2. BEERS, R.F., and SIZER, J.W. (1952). A spectrophotometric method of measuring the breakdown of hydrogen peroxide by catalase. J. Biol. Chem. 195, 133-140.
3. BONDY, S.C., and NADERI, S. (1994). Contribution of hepatic cytochrome P450 systems to the generation of reactive oxygen species. Biochem. Pharmacol. 48, 155-159.
4. BOYER, M., FRIEDLANDER, M., BANNAYNE, P., and ATKINSON, K. (1989). Hypercalcemia associated with mucinous adenocarcinoma of the ovary: a case report. Gynecol. Oncol. 35, 387-390.