scholarly journals Orotic Acid Added to Casein, but not to Egg Protein, Soy Protein, or Wheat Gluten Diets Increases 1,2-Diacylglycerol Levels and Lowers Superoxide Dismutase Activities in Rat Liver

2001 ◽  
Vol 65 (10) ◽  
pp. 2166-2173 ◽  
Author(s):  
Yoritaka AOYAMA ◽  
Mizuho WADA ◽  
Masashi MORIFUJI
Keyword(s):  
Superoxide Dismutase ◽  
Rat Liver ◽  
Soy Protein ◽  
Orotic Acid ◽  
Wheat Gluten ◽  
Egg Protein

Soy Protein Suppresses Gene Expression of Acetyl-CoA Carboxylase Alpha from Promoter PI in Rat Liver

2006 ◽  
Vol 70 (4) ◽  
pp. 843-849 ◽  
Author(s):  
Hisa AOKI ◽  
Kumi KIMURA ◽  
Kiharu IGARASHI ◽  
Asako TAKENAKA
Keyword(s):  
Gene Expression ◽  
Rat Liver ◽  
Soy Protein ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa

Photogeneration of Superoxide Anion upon Illumination of Purines and Pyrimidines in the Presence of Riboflavin: Structure-activity Relationships

1980 ◽  
Vol 43 (1) ◽  
pp. 19-20 ◽  
Author(s):  
MALGORZATA KORYCKA-DAHL ◽  
THOMAS RICHARDSON
Keyword(s):  
Superoxide Dismutase ◽  
Superoxide Anion ◽  
Orotic Acid ◽  
Imidazole Ring ◽  
Fluorescent Light ◽  
Carboxyl Group ◽  
Amino Group ◽  
Structure Activity ◽  
Related Compounds ◽  
Purines And Pyrimidines

Photogenerated superoxide anion might be involved in the oxidative deterioration of foods. For this reason, purines, pyrimidines and related compounds were illuminated with fluorescent light in the presence of riboflavin to examine their capacity to photogenerate superoxide anion (measured from suppression of its reduction of nitro blue tetrazolium by superoxide dismutase). Superoxide anion was photogenerated in the presence of guanine, xanthine, 6-thioguanine, thymine, uracil, 6-methyl uracil, orotic acid and 5- as well as 6-amino uracil but not in the presence of 24 other related compounds examined. Replacing the oxygen at the 6-position of guanine with sulfur or attachment of an amino group to the 5- or 6-carbon of uracil greatly increased superoxide anion generation as compared to guanine and uracil, respectively. The attachment of a carboxyl group at the 6-position of uracil augmented superoxide anion photogeneration to a much smaller extent and thymine and 6-methyl uracil did not yield any more superoxide anion than did uracil. In general, only those compounds which had an oxo group at the 6-position of purines or the 4-position of pyrimidines, and either an oxo or an amino group in the 2-position of either ring served as substrates for photogeneration of superoxide anion. Additionally, presence of purines and pyrimidines in an enol and/or amino form and an unsubstituted imidazole ring for purines were required for photogeneration of superoxide anion.

Design of novel edible hydrocolloids by structural interplays between wheat gluten proteins and soy protein isolates

2020 ◽  
Vol 100 ◽  
pp. 105395 ◽  
Author(s):  
Jian He ◽  
Ren Wang ◽  
Wei Feng ◽  
Zhengxing Chen ◽  
Tao Wang
Keyword(s):  
Soy Protein ◽  
Wheat Gluten ◽  
Protein Isolates ◽  
Gluten Proteins ◽  
Soy Protein Isolates

scholarly journals Molecular immunocytochemistry of the CuZn superoxide dismutase in rat hepatocytes.

1988 ◽  
Vol 107 (6) ◽  
pp. 2169-2179 ◽  
Author(s):  
L Y Chang ◽  
J W Slot ◽  
H J Geuze ◽  
J D Crapo
Keyword(s):  
Superoxide Dismutase ◽  
Rat Liver ◽  
Oxidant Stress ◽  
Rat Hepatocytes ◽  
Reaction Rates ◽  
Cytoplasmic Matrix ◽  
Cytosolic Proteins ◽  
Cuzn Superoxide Dismutase ◽  
O2 Production

The distribution of CuZn superoxide dismutase (SOD) molecules in subcellular organelles in rat liver hepatocytes was studied using integrated biochemical, stereological, and quantitative immunocytochemical techniques. A known concentration of purified CuZn SOD in 10% gelatin was embedded alongside the liver tissue for the calculation of CuZn SOD concentrations in hepatocyte organelles and total CuZn SOD in the rat liver. Most of the CuZn SOD was located in the cytoplasmic matrix (73.1%) and in the nucleus (11.9%) with concentrations of 1.36 and 0.71 mg/cm3, respectively. Lysosomes contained the highest concentration (5.81 mg/cm3). Only low concentrations were measured in mitochondria (0.21 mg/cm3). Membrane-bound spaces of rough endoplasmic reticulum (ER), smooth ER, and the Golgi system did not contain significant concentrations of the enzyme. By adding up the concentrations in all subcellular compartments, a total liver content of CuZn SOD was established from the immunocytochemical measurements (0.386 +/- 0.028 mg/gm liver) that agreed closely with those obtained by biochemical assays (0.380 +/- 0.058 mg/gm liver). The average distances between two CuZn SOD molecules can be calculated from enzyme concentrations. It was determined that CuZn SOD molecules in the cytoplasmic matrix and nucleus were 34 and 42 nm apart, respectively. In peroxisomes and mitochondria, average intermolecular distance increased to approximately 60 nm and increased to 136 nm in smooth ER. CuZn SOD is a relatively abundant protein in the cytosol of hepatocytes and its distribution overlaps with major sites of O2- production. The efficiency of protection CuZn SOD can provide to cytosolic proteins from attacks by superoxide anion depends on the rate of O2- production, distribution of CuZn SOD relative to cytosolic proteins, and the relative reaction rates between O2- with both cytosolic proteins and CuZn SOD. Future studies of these substrate-enzyme relationships in vivo can lead to a greater understanding of how cells handle oxidant stress.

Effects of estradiol benzoate and progesterone on superoxide dismutase activity in the rat liver

1997 ◽  
Vol 20 (4) ◽  
pp. 203-206 ◽  
Author(s):  
J. Kasapović ◽  
S. B. Pajović ◽  
D. T. Kanazir ◽  
J. V. Martinović
Keyword(s):  
Superoxide Dismutase ◽  
Rat Liver ◽  
Estradiol Benzoate ◽  
Superoxide Dismutase Activity
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