scholarly journals Properties of extracellular superoxide dismutase from human lung

1984 ◽  
Vol 220 (1) ◽  
pp. 269-272 ◽  
Author(s):  
S L Marklund
Keyword(s):  
Hydrogen Peroxide ◽  
Superoxide Dismutase ◽  
Human Lung ◽  
Sodium Dodecyl ◽  
Superoxide Dismutases ◽  
Extracellular Superoxide Dismutase ◽  
Order Of Magnitude ◽  
Cuzn Superoxide Dismutase ◽  
Very High

A further characterization of human extracellular superoxide dismutase is reported. The study was especially aimed at the interaction with substances known to interfere with CuZn superoxide dismutase and other superoxide dismutases. Extracellular superoxide dismutase is efficiently inhibited by cyanide and is about 3 times more sensitive than is human CuZn superoxide dismutase. The sensitivity to azide is much lower, but still about 3 times higher than that of human CuZn superoxide dismutase. Extracellular superoxide dismutase is about as rapidly inactivated by hydrogen peroxide as is CuZn superoxide dismutase. The sensitivity to diethyldithiocarbamate is very high and more than an order of magnitude larger than that of CuZn superoxide dismutase. Sodium dodecyl sulphate, under conditions suggested as being suitable for distinguishing between the insensitive CuZn superoxide dismutase and the sensitive Mn superoxide dismutase, efficiently inactivated extracellular superoxide dismutase. No antigenic similarities between extracellular superoxide dismutase and CuZn superoxide dismutase could be demonstrated. Anti-(extracellular superoxide dismutase) did not bind CuZn superoxide dismutase, and anti-(CuZn superoxide dismutase) did not bind extracellular superoxide dismutase.

An Inter-subunit Disulfide Bond Affects Affinity of Human Lung Extracellular Superoxide Dismutase to Heparin

2003 ◽  
Vol 37 (8) ◽  
pp. 823-827 ◽  
Author(s):  
Tomomi Ookawara ◽  
Hironobu Eguchi ◽  
Takako Kizaki ◽  
Chitose Nakao ◽  
Yuzo Sato ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Disulfide Bond ◽  
Human Lung ◽  
Extracellular Superoxide Dismutase

scholarly journals Hydrogen peroxide induce modifications of human extracellular superoxide dismutase that results in enzyme inhibition

Redox Biology ◽  
2013 ◽  
Vol 1 (1) ◽  
pp. 24-31 ◽  
Author(s):  
Randi H. Gottfredsen ◽  
Ulrike G. Larsen ◽  
Jan J. Enghild ◽  
Steen V. Petersen
Keyword(s):  
Hydrogen Peroxide ◽  
Superoxide Dismutase ◽  
Enzyme Inhibition ◽  
Extracellular Superoxide Dismutase

Superoxide dismutase fromAscaris suum

Parasitology ◽  
1988 ◽  
Vol 97 (2) ◽  
pp. 345-353 ◽  
Author(s):  
M. Sanchez-Moreno ◽  
M. Monteoliva ◽  
A. Fatou ◽  
M. A. García-Ruiz
Keyword(s):  
Hydrogen Peroxide ◽  
Superoxide Dismutase ◽  
Mitochondrial Fraction ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Superoxide Dismutases ◽  
Cytoplasmic Fraction ◽  
Sephadex Column ◽  
Ammonium Sulphate Precipitation ◽  
Electrophoretic Patterns

SummaryThree superoxide dismutases (SOD) (EC 1.15.1.1) were detected in homogenates ofAscaris suum. Each of the three forms of SOD was purified by a sequence of multiple differential centrifugations, ammonium sulphate precipitation, ion-exchange chromatography and G-75 Sephadex column chromatography. The three forms of SOD were present in different cellular locations; one in the cytoplasmic fraction, sensitive to cyanide and hydrogen peroxide, and two in the mitochondrial fraction, one of which was cyanide sensitive. The SOD forms presented clear differences in their electrophoretic patterns. The sexual organs of females showed the highest SOD activities of all the tissues examined. The finding of such high levels of superoxide dismutase inA. suumreflects the importance of this enzyme in the metabolism of this helminth parasite.

Characterization of Heparin Binding of Human Extracellular Superoxide Dismutase†

Biochemistry ◽  
2000 ◽  
Vol 39 (1) ◽  
pp. 230-236 ◽  
Author(s):  
Aivar Lookene ◽  
Peter Stenlund ◽  
Lena A. E. Tibell
Keyword(s):  
Superoxide Dismutase ◽  
Extracellular Superoxide Dismutase ◽  
Heparin Binding

scholarly journals Cloning and expression analysis of Drosophila extracellular Cu Zn superoxide dismutase

2014 ◽  
Vol 34 (6) ◽  
Author(s):  
Michael J. Blackney ◽  
Rebecca Cox ◽  
David Shepherd ◽  
Joel D. Parker
Keyword(s):  
Superoxide Dismutase ◽  
Expression Analysis ◽  
Splice Variants ◽  
Cloning And Expression ◽  
Superoxide Dismutases ◽  
Extracellular Superoxide Dismutase ◽  
Specific Expression ◽  
Mrna Splice ◽  
Enhanced Resistance

Extracellular superoxide dismutase (SOD3) in Drosophila is characterized for mRNA splice variants and sex-specific expression. A SOD3 mutant reveals no effect on longevity, enhanced resistance to paraquat and H202, and provided evidence suggesting an interaction with other superoxide dismutases.

scholarly journals Extracellular superoxide dismutase and other superoxide dismutase isoenzymes in tissues from nine mammalian species

1984 ◽  
Vol 222 (3) ◽  
pp. 649-655 ◽  
Author(s):  
S L Marklund
Keyword(s):  
Skeletal Muscle ◽  
Superoxide Dismutase ◽  
Tissue Distribution ◽  
Mammalian Species ◽  
Superoxide Dismutase Activity ◽  
Rat Tissues ◽  
Extracellular Superoxide Dismutase ◽  
Liver And Kidney ◽  
Cuzn Superoxide Dismutase

The contents of extracellular superoxide dismutase, CuZn superoxide dismutase and Mn superoxide dismutase were determined in tissues from nine mammalian species. The pattern of CuZn superoxide dismutase distribution was similar in all species, with high activity in metabolically active organs such as liver and kidney and low activity in, for example, skeletal muscle. Mn superoxide dismutase activity was high in organs with high respiration, such as liver, kidney, and myocardium. Overall the Mn superoxide dismutase activity in organs was almost as high as the CuZn superoxide dismutase activity. The content of extracellular superoxide dismutase was, almost without exception, lower than the content of the other isoenzymes. The pattern of tissue distribution was distinctly different from those of CuZn superoxide dismutase and Mn superoxide dismutase. The tissue distribution of extracellular superoxide dismutase differed among species, but in general there was much in lungs and kidneys and little in skeletal muscle. In man, pig, sheep, cow, rabbit and mouse the overall tissue extracellular superoxide dismutase activities were similar to each other, whereas dog, cat and rat tissues contained distinctly less. There was no general correlation between the tissue extracellular superoxide dismutase activity of any of the various species and the variable plasma activity. The ratio between the plasma and the overall tissue activities was high, for some species over unity, providing further evidence for the notion that one role of extracellular superoxide dismutase is as a plasma protein.

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