The effect of sulfhydryl compounds on the catalytic activity of Cu, Zn-superoxide dismutase purified from rat liver

1985 ◽  
Vol 41 (11) ◽  
pp. 1416-1419 ◽  
Author(s):  
T. Hoshino ◽  
Y. Ohta ◽  
I. Ishiguro
Keyword(s):  
Superoxide Dismutase ◽  
Catalytic Activity ◽  
Rat Liver ◽  
Sulfhydryl Compounds

Eritadenines - Novel type of potent inhibitors of S-adenosyl-L-homocysteine hydrolase

1982 ◽  
Vol 47 (1) ◽  
pp. 167-172 ◽  
Author(s):  
Ivan Votruba ◽  
Antonín Holý
Keyword(s):  
Catalytic Activity ◽  
Rat Liver ◽  
Hydrolytic Reaction

Rat liver SAH-hydrolase is strongly inhibited by four stereoisomeric 4-(adenin-9-yl)-2,3-dihydroxybutyric acids (eritadenines). D-Eritadenine, which is the most effective of the four, inactivates the catalytic activity of SAH-hydrolase at IC50 = 1.2 .10-8 mol l-1 in the hydrolytic reaction. The enzyme is irreversibly inhibited (τ/2 = 1.6 min). The inactivation activity decreases in the order D-erythro(2R, 3R) L-erythro(2S, 3S) threo(2S, 3R) threo(2R, 3S) configuration.

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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