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Query: UNIPROT:P04040 (
Catalase
)
3,577
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
We studied the effect of
water
-soluble antioxidants on the cell energetics in multiple organs in rats in response to a 20% total body surface area third-degree burn injury. Liver, lung, and heart tissue were studied. Cell energetics were measured as tissue energy charge potential (ECP), adenosine triphosphate (ATP) content, and total adenine nucleotides. The enzymatic antioxidant catalase was used as a marker of endogenous cell antioxidant activity, especially to hydrogen peroxide. The
water
-soluble antioxidants glutathione, N-acetylcysteine, and vitamin C were given orally beginning at the time of burn injury and for the 6-day study period. All rats were fluid resuscitated according to the Parkland formula. The mortality rate was 0% for this size burn. The ECP in lung, liver, and heart, was normal on day 1 after the burn injury. However, the ECP was significantly decreased from the controls in the liver by day 3, with a peak decrease at day 6 as inflammation increased. A decrease in the heart ECP occurred between day 3 and day 6. Total adenine nucleotides did not decrease, indicating the decrease in ECP to be the result of a decrease in ATP. ECP remained normal in the lung.
Catalase
was also decreased in the liver and the heart and remained at normal levels in the lung. The decrease in the liver and heart ECP and ATP was eliminated with the oral antioxidant administration after the burn injury. We conclude that a modest burn injury decreases cellular energy charge in the heart and liver not immediately after burn but 3 to 6 days later. The decrease in antioxidant activity precedes the decrease in ECP. The lung appears to be protected.
Water
-soluble antioxidants, given after burn injury, prevent the altered cell energetics-strongly suggesting a cause-and-effect relationship between increased oxidant release with inflammation, decreased antioxidant activity, and altered cell energetics.
...
PMID:Antioxidants prevent the cellular deficit produced in response to burn injury. 888 59
Hydrogen peroxide (H2O2) is a reactive oxygen species that at low concentration is toxic to sperm. H2O2 inhibits not only sperm viability but also the acrosome reaction, sperm-egg binding, and oocyte penetration.
Catalase
activates the decomposition of H2O2 into
water
and oxygen, thus removing an initiator of free radical chain reactions leading to lipid peroxidation. Since the oviduct is known to enhance sperm survival, we hypothesized that it might secrete catalase. We found that oviductal fluid, harvested from washed cells collected at the slaughterhouse, possessed catalase-specific activity that varied during the estrous cycle.
Catalase
activity increased during the cycle and reached its maximal level just before ovulation (Days 18-20). No significant difference in activity was seen between fluid from the isthmus and that from the ampulla. Indirect immuno-staining of spermatozoa incubated in the oviductal fluid revealed the association of catalase in the region of the acrosomal cap. Addition of a commercial antibody directed against bovine liver catalase completely inhibited catalase activities from the oviductal fluid.
Catalase
activity was also detected in porcine oviductal fluid, human oviductal fluid, and cervical mucus. Western blots of oviductal fluid probed with the anti-catalase antibody revealed two major bands at 60 and 40 kDa. An immunoaffinity column was used to purify oviductal catalase, showing a unique band at about 60 kDa when analyzed by SDS-PAGE. The purified protein was incubated with bovine, boar, and human sperm, and Western blots of these sperm after several washes detected a band at 60 kDa, indicating that the protein was bound to sperm membranes. However, bovine liver catalase did not bind to sperm. Since H2O2 is one of the key reactants in the chain reaction of free radical production, this enzyme may play an important role in sperm survival within the female tract.
...
PMID:Binding of a bovine oviductal fluid catalase to mammalian spermatozoa. 951 Sep 62
Catalase
(
CAT
) activity in ground beef and pork was determined on samples cooked from 60 to 71.1 degrees C. One-gram samples of ground round (4% fat), hamburger (24% fat), and commercial pork sausage (38%fat) were cooked in a controlled-temperature waterbath at 65, 68.3 and 71 degrees C. Chilled samples were immersed in direct contact with the cooking
water
; the test samples were removed every 15 s and immediately immersed in an ice-
water
bath (O to 1 degrees C) to quick-chill the samples to prevent temperature over-run. Samples retained high (HMB value 20+, over range)
CAT
activity through 90, 60, and 45 s at 65, 68.3, and 71 degrees C, respectively, before showing rapid activity decreases. Four USDA-FSIS approved meat patty heating processes (66.1 degrees C, 41 s; 67.2 degrees C, 26 s; 68.3 degrees C, 16 s; and 69.4 degrees C, 10 s) were analyzed for
CAT
activity in meat frozen prior to cooking was slightly lower (P < 0.05) than in degrees C meat.
CAT
activity decreased (P < 0.05) among meat treated at 66.1 degrees C for 41 s, at 67.2 degrees C for 26 s, and at 68.3 degrees C for 16 s, but the treatment at 68.3 degrees C for 16 s was not different (P < 0.05) from that at 69.4 degrees C for 10 s. These results show this rapid (20 to 25 min)
CAT
activity test could be used to establish activity values at specific end-point temperatures for model heat-processed ground beef or sausage products and may be useful to USDA FSIS process inspectors and food processors in quality assurance and HACCP (hazard analysis critical control points) programs for thermal input verification.
...
PMID:Evaluation of a rapid method for measurement of catalase activity in cooked beef and sausage. 970 92
Electron spin resonance spin trapping was utilized to investigate free radical generation from cobalt (Co) mediated reactions using 5,5-dimethyl-1-pyrroline (DMPO) as a spin trap. A mixture of Co with
water
in the presence of DMPO generated 5,5-dimethylpyrroline-(2)-oxy(1) DMPOX, indicating the production of strong oxidants. Addition of superoxide dismutase (SOD) to the mixture produced hydroxyl radical (.OH).
Catalase
eliminated the generation of this radical and metal chelators, such as desferoxamine, diethylenetriaminepentaacetic acid or 1,10-phenanthroline, decreased it. Addition of Fe(II) resulted in a several fold increase in the .OH generation. UV and O2 consumption measurements showed that the reaction of Co with
water
consumed molecular oxygen and generated Co(II). Since reaction of Co(II) with H2O2 did not generate any significant amount of .OH radicals, a Co(I) mediated Fenton-like reaction [Co(I) + H2O2-->Co(II) + .OH + OH-] seems responsible for .OH generation. H2O2 is produced from O2.- via dismutation, O2.- is produced by one-electron reduction of molecular oxygen catalyzed by Co. Chelation of Co(II) by biological chelators, such as glutathione or beta-ananyl-3-methyl-L-histidine alters, its oxidation-reduction potential and makes Co(II) capable of generating .OH via a Co(II)-mediated Fenton-like reaction [Co(II) + H2O2-->Co(III) + .OH + OH-]. Thus, the reaction of Co with
water
, especially in the presence of biological chelators, glutathione, glycylglycylhistidine and beta-ananyl-3-methyl-L-histidine, is capable of generating a whole spectrum of reactive oxygen species, which may be responsible for Co-induced cell injury.
...
PMID:Cobalt-mediated generation of reactive oxygen species and its possible mechanism. 972 Mar 10
The results of studies on producing the biocatalyst based on catalase immobilized in the fibers from triacetate are presented. The catalase producer is Penicillium fungus.
Catalase
was produced by precipitation with the use of ethyl alcohol from the cultural fluid with separate and unseparate mycelium. The highest activity of catalase in the cultural fluid is seen on the nutrient medium containing 4% of carbon source. For immobilization the
water
solution of enzyme was concentrated in the vacuum-rotor evaporator at temperature of 25 degrees C. The enzyme was included in the structure of fibers during the process of their formation. Of the fiber-producing polymers (cellulose triacetate, chlorine, polysulphone) the most enzymatic activity has the catalase-containing fibers derived from the cellulose triacetate, in this case, the fine fibers of biocatalyst have the higher specific activity. It is established that the fibers obtained by using catalase of microbiological origin possess high stability and their activity does not practically change in the aqueous environment. The unpurified catalase is one and a half higher than at purified catalase. Under laboratory conditions there turned out the experimental batches of fibers and there conducted their endurance tests.
Catalase
included in cellulase triacetate has effectively functioned during a period of 2 years purifying the distilled
water
containing 50 mg/l of hydrogen peroxide.
...
PMID:[Immobilized catalase in water purification systems]. 985 84
Phenotypic and phylogenetic studies were performed with two strains (OCh 317T and OCh 318; T = type strain) of aerobic chemoheterotrophic bacteriochlorophyll-containing bacteria isolated from
water
of a saline lake located on the west coast of Australia. Both strains were Gram-negative, short rods and were motile by means of polar flagella.
Catalase
, oxidase, nitrate reductase, phosphatase and urease were produced. The cells utilized D-glucose, citrate, glycolate, pyruvate and ethanol. Acids were produced from L-arabinose, D-fructose, D-galactose, D-glucose, D-ribose and D-xylose. The strains could grow in media containing 0.5-7.5% NaCl. Bacteriochlorophyll a was synthesized under aerobic conditions. The results of 16S rRNA gene sequence comparisons revealed that strain OCh 317T represented a new lineage in the alpha-3 group of the class Proteobacteria. Strains OCh 317T and OCh 318 were identified as strains of the same species because of their very similar phenotypic characteristics and their previously described high DNA-DNA homology. Therefore, it was concluded that the two strains should be assigned to a new genus and species, for which the name Rubrimonas cliftonensis is proposed. The type strain is OCh 317T (= JCM 10189T).
...
PMID:Rubrimonas cliftonensis gen. nov., sp. nov., an aerobic bacteriochlorophyll-containing bacterium isolated from a saline lake. 1002 64
Comparative studies were performed on the antioxidant enzyme activities and thiobarbituric acid reactive substance (TBARS) concentration in liver and red cells of two groups of rainbow trout (Oncorhynchus mykiss). The fish of the first group were cultured in freshwater and the others were adapted to sea-
water
by by being transferred from freshwater at 5-6 months of age.
Catalase
(
CAT
), glutathione peroxidase (GPX), and glutathione S-transferase (GST) activities were significantly higher in hepatic and extrahepatic tissues in both of the fish groups. Superoxide dismutase (SOD) activities were found lower in the seawater-adapted trout than in the freshwater-cultured trout. In both tissues, TBARS were found significantly higher in the seawater-adapted trout than in the freshwater trout. It was also observed that the red cells of the seawater-adapted trout were much more resistant to oxidative stress than the red cells of the freshwater-cultured trout. The results implicate that antioxidant capacities in the seawater-adapted trout and freshwater trout may be related to physical and chemical characteristics of the environment.
...
PMID:A comparative study of antioxidant enzyme activities in freshwater and seawater-adapted rainbow trout. 1048 21
Two broccoli cultivars which have been previously found to have large differences in yellowing susceptibility were studied to determine if there was a relationship between antioxidant capability and chlorophyll loss at a simulated retail display temperature. Greenbelt cultivar retained a stable chlorophyll content over 4 days at 13 degrees C, while Emperor cultivar showed a constant decline in chlorophyll content. These differences were not related to differences in
water
loss. Superoxide dismutase (SOD) and peroxidase (POD) activities were approximately 30% higher in Greenbelt than in Emperor. The ratio of superoxide dismutase to peroxidase activity was also lower in Greenbelt. The susceptibility of Emperor to oxygen radical damage and lipid peroxidation is expected to be higher since an excessive SOD activity, with respect to POD activity, can potentially lead to enhanced hydroxyl radical formation.
Catalase
(
CAT
) activity was higher in Emperor, suggesting that catalase is not important in providing resistance to chlorophyll loss in broccoli.
Water
soluble, nonenzymatic antioxidant activity was similar for both cultivars. These results support the hypothesis that antioxidant protection offered by superoxide dismutase and peroxidase is important to retention of green color in broccoli.
...
PMID:Differences in Chlorophyll Loss at 13 degrees C for Two Broccoli (Brassica oleracea L.) Cultivars Associated with Antioxidant Enzyme Activities. 1055 90
The deficiency of methionine, an essential amino acid, is associated with cardiovascular lesions. Because different types of cardiac pathologies are caused by a decrease in antioxidants, we examined the effects of methionine on myocardial antioxidant enzymes in hemodynamically assessed rats that were treated with methionine (10 mg/ml) in drinking
water
for 12, 24, and 48 h. Glutathione peroxidase (GSHPx) activity was significantly increased to 150.5 +/- 12.2 and 191.7 +/- 13.7% of the control value at 12 and 24 h, respectively, followed by a decline to 120 +/- 24.6% at 48 h. The mRNA levels of GSHPx at these time points were 151.2 +/- 12.0, 218.7 +/- 35.3, and 173.5 +/- 25.2%, respectively. Superoxide dismutase (SOD) activity was 144.3 +/- 3.7, 114.3 +/- 10.1, and 143.1 +/- 11. 2% at 12, 24, and 48 h, respectively.
Catalase
(Cat) activity was 272.4 +/- 5.4, 237.8 +/- 16.6, and 224.1 +/- 17.3% of the control value. The expression of Cat and SOD mRNA was unchanged at 12, 24, and 48 h. The lipid peroxidation was decreased by 24.4 +/- 11.2, 54. 9 +/- 0.1, and 6.4 +/- 2.1% at 12, 24, and 48 h, respectively. Methionine had no effect on the ventricular or aortic pressures, heart rate, and myocardial glutathione levels at any of the time points. The study shows that methionine has a significant effect on the myocardial antioxidant enzyme activities, and only changes in GSHPx enzyme activity correlated with the mRNA changes. These antioxidant changes may have a role in the beneficial effects of methionine in pathological rather than physiological conditions.
...
PMID:Effects of methionine on endogenous antioxidants in the heart. 1060 Aug 29
Catalase
(E.C. 1.11.1.6) was purified from human erythrocytes and crystallized in three different forms: orthorhombic, hexagonal and tetragonal. The structure of the orthorhombic crystal form of human erythrocyte catalase (HEC), with space group P2(1)2(1)2(1) and unit-cell parameters a = 84.9, b = 141.7, c = 232.5 A, was determined and refined with 2.75 A resolution data. Non-crystallographic symmetry restraints were employed and the resulting R value and R(free) were 0.206 and 0.272, respectively. The overall structure and arrangement of HEC molecules in the orthorhombic unit cell were very similar to those of bovine liver catalase (BLC). However, no NADPH was observed in the HEC crystal and a
water
was bound to the active-site residue His75. Conserved lattice interactions suggested a common growth mechanism for the orthorhombic crystals of HEC and BLC.
...
PMID:Structure of human erythrocyte catalase. 1066 17
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