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PubMed2005

Changes in the activity of amylase, peroxidase and catalase in beech (Fagus orientalis Lipsky) during dormancy and growth.

Activities of peroxidase, amylase and catalase were analyzed on beech (Fagus orientalis Lipsky) during one year to determine relationship between these enzymes with the period of dormancy and growing season. Results showed that amylase activity was high but catalase and peroxidase activities were low during the growing season. Peroxidase and catalase activities increased from July to November whereas amylase activity started to decrease at the same time, which means that the plants were prepared themselves to be dormant and the hardening was happened. The peroxidase maximum activity was in November, which is an important sign of dormancy and completing hardening in plant. The dormancy released from February along with decrease of catalase activity. At the beginning of growing season, correlation between amylase and catalase was increased. Amylase activity also increased gradually. No significant correlation between amylase-catalase and amylase-peroxidase activities was found at the period of dormancy. In our study, we found that the seasonal activity of enzymes such as peroxidase, catalase, and amylase, also correlation between these enzymes could be an important factor for the detection the period of dormancy and growing season.

Amylases↗
PubMed1991

Effect of a protease inhibitor on the stability of catalase in liver and blood from acatalasemic and normal mice.

Effects of Gabexate mesilate (GM) (([ethyl-4-(6-guanidino hexanoyloxy) benzoate] methane sulfonate)), a protease inhibitor, on the activities of catalase in liver, erythrocytes and reticulocytes from acatalasemic mice were examined. Preincubation without GM at 37 degrees C for 160 min lowered the catalase activities of liver, erythrocytes and reticulocytes from acatalasemic mice, to 24%, 40% and 10% of the initial levels, respectively. But, preincubation with GM at 37 degrees C for 160 min delayed the rapid decrease in activities of residual catalases in the liver, erythrocytes and reticulocytes of acatalasemic mice to 65%, 93% and 85% of the initial values, respectively. At 20 degrees C or below, no reduction in catalase activity of reticulocytes from acatalasemic mice occurred with or even without GM. At pH 5.0, the decrease in catalase activity of acatalasemic mice was small both in the presence and the absence of GM. In the alkaline range, the reduction in the enzyme activity of the mutant mice without GM was enhanced with increase in pH values up to 8.5. But the presence of GM during preincubation at pH 7.5, retained the catalase activity of acatalasemic mice, to 64% of the activity at pH 6.5. These data suggest that some factors affected by GM, might be responsible for the low stability and activity of catalase in the acatalasemic mice.

Acatalasia↗
PubMedDate not supplied

Cytoplasmic catalase and ghostlike peroxisomes in the liver from a child with atypical chondrodysplasia punctata.

In the liver biopsy from an 8.5-year-old girl with the biochemical characteristics of rhizomelic chondrodysplasia punctata (RCDP), but with normal limbs, normal catalase-containing peroxisomes were absent. Light microscopy after diaminobenzidine staining for catalase activity (the peroxisomal marker enzyme) and immunostaining against catalase protein indicated a cytosolic localization of the enzyme. By electron microscopy, rare and extremely large, irregularly shaped vesicles were found in the parenchymal cells. The three peroxisomal beta-oxidation enzymes (acyl-CoA oxidase, bi(tri)functional enzyme, and 3-ketoacyl-CoA thiolase) and alanine-glyoxylate aminotransferase were immunolocalized in these organelles. However, a weak to negative label was obtained after staining against catalase. Diaminobenzidine staining demonstrated a minimal catalase reaction product in some vesicles only. Morphometry revealed a corrected mean d-circle of 1.44 microns and a maximum d-circle of 2.767 microns (controls: 0.635 microns and 1.027 microns, respectively). Numerical, volume, and surface densities were reduced to 3%, 41%, and 17% of control values, respectively. The large size, irregular shape, and rarity of the organelles are morphologic features of peroxisomal "ghosts." It seems that in this patient, apart from the known peroxisomal defects in RCDP, catalase incorporation into the peroxisomes is impaired together with a normal proliferation (division) of the organelles. In the cultured skin fibroblasts from the patient, however, immuno-electron microscopy showed normal catalase-containing peroxisomes in apparently normal numbers.

Catalase↗
PubMed1989

Similarities between catalase and cytosolic epoxide hydrolase.

Cytosolic epoxide hydrolase, measured as trans-stilbene oxide hydrolase activity, was isolated and purified from human and guinea pig liver cytosol. Antiserum to the guinea pig liver preparation reacted strongly with bovine liver catalase. We determined that this lack of selectivity of the antiserum was due to catalase contamination of the epoxide hydrolase preparation. We also determined that several commercial catalase preparations are contaminated with cytosolic epoxide hydrolase. Our human epoxide hydrolase preparation contained no detectable catalase contamination, yet antiserum to this protein also cross-reacted slightly with catalase, indicating some intrinsic similarity between the two enzymes. We conclude that catalase and cytosolic epoxide hydrolase contain some similar immunogenic epitopes, and we surmise that similarities between the subunits of these two enzymes may lead to their partial copurification. Functional similarities between the two enzymes are also demonstrated, as several compounds that inhibit catalase are also shown to inhibit cytosolic epoxide hydrolase activity in the same concentration range and rank order.

Amino Acids↗
PubMed2001

Molecular cloning, sequencing analysis and expression of the catalase-peroxidase gene from Halobacterium salinarum.

The gene encoding catalase-peroxidase was cloned from chromosomal DNA from the Archaea, Halobacterium salinarum. The nucleotide sequence of a 3.5 kb fragment, containing the catalase-peroxidase gene and its flanking regions was determined. A 2.16 kb open reading frame was obtained, encoding the enzyme which was comprised of 720 amino acid residues with a calculated molecular weight of 80 kDa. The deduced amino acid sequence of the H. salinarum catalase-peroxidase showed a high degree of identity to other bifunctional catalase-peroxidases. A transcriptional start site was identified 183 bp upstream of the translational start codon. Southern blot analysis indicated that catalase-peroxidase was a single copy gene. The Archaeal catalase-peroxidase gene was expressed in Escherichia coli, and the expressed fusion protein exhibited both catalase and peroxidase activities.

Amino Acid Sequence↗
PubMed2006

Nitrotyrosine proteome survey in asthma identifies oxidative mechanism of catalase inactivation.

Reactive oxygen species and reactive nitrogen species produced by epithelial and inflammatory cells are key mediators of the chronic airway inflammation of asthma. Detection of 3-nitrotyrosine in the asthmatic lung confirms the presence of increased reactive oxygen and nitrogen species, but the lack of identification of modified proteins has hindered an understanding of the potential mechanistic contributions of nitration/oxidation to airway inflammation. In this study, we applied a proteomic approach, using nitrotyrosine as a marker, to evaluate the oxidation of proteins in the allergen-induced murine model of asthma. Over 30 different proteins were targets of nitration following allergen challenge, including the antioxidant enzyme catalase. Oxidative modification and loss of catalase enzyme function were seen in this model. Subsequent investigation of human bronchoalveolar lavage fluid revealed that catalase activity was reduced in asthma by up to 50% relative to healthy controls. Analysis of catalase isolated from asthmatic airway epithelial cells revealed increased amounts of several protein oxidation markers, including chloro- and nitrotyrosine, linking oxidative modification to the reduced activity in vivo. Parallel in vitro studies using reactive chlorinating species revealed that catalase inactivation is accompanied by the oxidation of a specific cysteine (Cys(377)). Taken together, these studies provide evidence of multiple ongoing and profound oxidative reactions in asthmatic airways, with one early downstream consequence being catalase inactivation. Loss of catalase activity likely amplifies oxidative stress, contributing to the chronic inflammatory state of the asthmatic airway.

Adult↗
PubMed1999

Isolation and characterization of the catalase gene from Rhizobium sp. SNU003, a root nodule symbiont of Canavalia lineata.

A catalase gene from Rhizobium sp. SNU003, a root nodule symbiont of Canavalia lineata, was cloned and its nucleotide sequence was determined. The Rhizobium DNA of about 280 bp was amplified using two PCR primers synthesized from the conserved sequences of the type I catalase gene. The nucleotide sequence of the amplified fragment revealed three regions that were conserved in the catalase, showing it as being part of the catalase gene. A genomic Southern hybridization using this fragment as a probe showed that the 5.5 kb PstI, 1.8 kb EcoRI, and 0.7 kb StyI fragments hybridized strongly with the probe. The Rhizobium genomic library constructed into the EMBL3 vector was screened, and one catalase clone was selected. The nucleotide sequence of the 5.5 kb PstI fragment from the clone revealed an open reading frame of 1455 bp, encoding a polypeptide of 485 amino acids with a molecular mass of 54,958 Da and a pI of 6.54. The predicted amino acid sequence of the catalase is 66.3% identical to that of Bacteroides fragilis, but was only 53.3% identical to the Rhizobium meliloti catalase.

Amino Acid Sequence↗
PubMed1976

Behavior of rat liver catalase during electrophoresis in a pH gradient.

Investigations were conducted on the distribution of rat liver catalase subsequent to electrofocusing in a pH gradient. Differences were observed depending on the enzyme being extracted from the total mitochondrial fraction, from the supernatant of the homogenate or from purified peroxisomes. Catalase solubilized from the total mitochondrial fraction exhibits an apparent isoelectric point lower than that of catalase derived from the supernatant. Catalase released from purified peroxisomes shows a behavior similar to that of the supernatant catalase. It has been concluded that, in a total mitochondrial fraction, a factor is present that alters the electric charge of the catalase molecule during or after the extraction of the enzyme. This factor is probably associated with lysosomes existing together with peroxisomes and mitochondria in a total mitochondrial fraction. As a matter of fact, the addition of an extract of purified lysosomes to purified peroxisomes or to supernatant will cause a shift towards a more acid pH of catalase distribution subsequent to electrofocalization.

Animals↗
PubMed1999

Acute lead acetate administration potentiates ethanol-induced locomotor activity in mice: the role of brain catalase.

It has been proposed that brain catalase plays a role in the modulation of some psychopharmacological effects of ethanol. The acute administration of lead acetate has demonstrated a transient increase in several antioxidant cell mechanisms, including catalase. In the present study, we investigated the effects of acute lead acetate administration on ethanol-induced behavior, brain catalase activity, and the relation between both effects. Lead acetate (100 mg/kg) or saline was injected intraperitoncally in mice. At different intervals of time (1, 3, 5, 7, 9, or 11 days) after this treatment, ethanol (2.5 g/kg) was injected intraperitoneally and the mice were placed in open field chambers. Results indicated that the locomotor activity induced by ethanol was significantly increased. Maximum ethanol-induced locomotion increase (70% more activity than control animals) was found in animals treated with lead acetate 7 days before ethanol administration. Total brain catalase activity in lead-pretreated animals also showed a significant induction, which was maximum 7 days after lead administration. A significant correlation was found between both effects of locomotor and catalase activity. In a second study, the effect of lead administration on d-amphetamine (2.0 mg/kg) and tert-butanol-(0.5 g/kg) induced locomotor activity was investigated. Lead acetate treatment did not affect the locomotion induced by these drugs. These data suggest that brain catalase is involved in ethanol's effects. They also provide further support for the notion that acetaldehyde may be produced directly in the brain via catalase and that it may be a factor mediating some of ethanol's central effects.

Animals↗
PubMedDate not supplied

[Blood catalase activity in brain tumors during the postoperative period].

Proceeding from the current ideas on the significance of the catalase in the oxidative phosphorylation, oxygenation and desoxygenation of hemoglobin the activity of the above enzyme was studied in the blood of 60 patients with brain tumours. It was found that prior to a surgical intervention the catalase activity at the rate per 1 g of hemoglobin (the catalase index-CI) varied within the same range in patients with brain tumours of a different histological structure (meningiomas, adenomas of the pituitary, gliomas, metastases of cancer). The catalase index of the patients' blood does not differ from that in healthy individuals. In the post-operative period the catalase index rises right from the first days, paralleling the development of a general reaction to the damage. There exists a correlation between a fall in the level of hemoglobin and a rise of the catalase index, which apparently, has a compensatory significance. An investigation of the catalase in the clinical picture of the stress-syndrome may be of use for prognostic purposes.

Adenoma↗
PubMed1976

Glomerular permeability to proteins. Effects of hemodynamic factors on the distribution of endogenous immunoglobulin G and exogenous catalase in the rat glomerulus.

The distribution of endogenous immunoglobulin G (IgG) and exogenous catalase was delineated in the rat glomerulus under normal and abnormal hemodynamic conditions. IgG was identified by an ultrastructural immunoperoxidase technique using antirat IgG Fab fragments conjugated to horseradish peroxidase; catalase was identified by a cytochemical reaction. When superficial glomeruli in anesthetized Munich-Wistar rats were rapidly fixed in situ by dripping glutaraldehyde onto the renal surface, IgG and catalase were largely confined to the glomerular capillary lumen, with only small amounts in the lamina rara interna immediately beneath the endothelial fenestrae, and none deeper in the basement membrane (GBM) or in the urinary space. If cortical tissue was subjected to routine immersion fixation, or if fixation was performed in situ after ligation of the renal artery, IgG and catalase were found throughout the GBM but not in the urinary space. If fixation was performed in situ after ligation of the renal artery and vein (or artery, vein, and ureter), IgG and catalase were found in the GBM and in the urinary space. If blood flow was restored for 10 minutes after 5 minutes of occlusion of the renal artery and vein, the distribution of IgG and catalase returned to that seen during good blood flow, i.e. neither showed significant penetration beyond the endothelial layer. Thus, as was found previously for albumin, glomerular barrier function for IgG and catalase depends upon the maintenance of normal blood flow conditions. We propose that such conditions impose functional restrictions may be mediated by molecular sieving phenomena during normal ultrafiltration across the GBM, perhaps in association with concentration-polarization or charge effects or both. The epithelial slit pores may significantly modulate solute flux across the GBM by controlling the over-all rate of hydrodynamic flow during ultrafiltration.

Animals↗
PubMedDate not supplied

[Effect of aminotriazole on the activity of catalase and glucose-6-phosphate dehydrogenase in tissues of two frog species--Rana ridibunda and Rana esculenta].

Changes of the activity of catalase and glucose-6-phosphate dehydrogenase (G6PDH) during 48 hrs after intraperitoneal injection of 1.0, 0.5 and 0.1 mg aminotriazole per gram of body weight of two frog species as well as catalase inhibition by aminotriazole in vitro were investigated. Both aminotriazole concentration and species affiliation affected the catalase inhibition. The sensitivity of catalase from different tissues was decreased in the order: liver--kidney--lung--muscle--brain. The constant of half inhibition of lung catalase was significantly lower than that of liver and kidney catalase. The activity of G6PDH of AMT-treated frogs R. esculenta was higher comparing to control group. Possible ways of compensation of antioxidant defense under catalase inhibition are discussed.

Amitrole↗
PubMed2006

[Hydrogen sulphide water balneum effect on erythrocyte catalase activity in patients with rheumatoid arthritis--in vitro study].

The aim of the study was to investigate, in vitro, hydrogen sulphide water (HSW) balneum effect on erythrocyte catalase activity in patients with rheumatoid arthritis. Erythrocytes from twenty nine consecutive patients with rheumatoid arthritis (11 men, 18 women) aged 54 years were obtained. The control group comprised of 30 healthy subjects with a mean age of about 40 years. Patients with rheumatoid arthritis were subdivided into two groups twice: with active disease (18 patients) and in remission (11 patients), and secondly into patients receiving (21 subjects) and not receiving (8 subjects) non-steroidal anti-inflammatory drugs. For erythrocyte catalase activity evaluation, method of Beers and Sizer was used. Catalase activity was assessed after 5, 10, 15, and 20 minutes erythrocytes incubation with HSW. The mean baseline erythrocyte catalase activity (to) was in rheumatoid arthritis patients of about 7.79 +/- 1.39 U/gHb and was significantly higher than in the control group: 6.96 +/- 2.68 U/gHb (p < 0.05). After 5 minutes incubation with HSW (t5) erythrocyte catalase activity increased, in rheumatoid arthritis patients to 8.21 +/- 1.77 U/gHb, after 10 minutes (t10) was 8.14 +/- 2.25 U/gHb, in control group: 7.58 +/- 2.50 U/gHb and 7.68 +/- 3.22 U/gHb, respectively. However the difference was not statistically significant. After 20 minutes of incubation (t20) erythrocyte catalase activity was the highest in the patients with active rheumatoid arthritis (8.33 +/- 1.96 U/gHb) and differed significantly from the patients in remission (6.69 +/- 1.27 U/gHb) and from patients not receiving non-steroidal anti-inflammatory drugs (6.04 +/- 1.08 U/gHb). In rheumatoid arthritis patients erythrocyte catalase activity was higher when compared with control group and increased during incubation with HSW. It seems HSW balneum produce an antioxidant effect on erythrocyte status in patients with rheumatoid arthritis.

Adult↗
PubMed1991

Vector-mediated overexpression of catalase A in the yeast Saccharomyces cerevisiae induces inclusion body formation.

To study the morphological effects of overexpression of catalase A in yeast, the gene coding for catalase A was introduced into Saccharomyces cerevisiae on a multicopy vector. After induction of microbody biogenesis and catalase A expression by growth on oleic acid as sole carbon source, cells were analyzed by immunofluorescence and immunoelectron microscopy. In addition, overexpression of catalase A was studied by quantitative immunoblotting and by activity measurement. Quantitative immunoblotting resulted in a 16-fold difference between immunoreactive material from transformed and non-transformed cells. An 18-fold increase of enzyme activity was measured in transformed cells due to overexpression of catalase A from plasmid pAH521. Immunofluorescent staining of semithin sections of Lowicryl HM20-embedded cells with anti-catalase localized peroxisomes and--at a low percentage--larger particles. By immunoelectron microscopy, these larger structures could be identified as agranular, electron-dense aggregates which are morphologically clearly distinct from the cytoplasm and not bounded by a membrane. These structures, which have been named inclusion bodies, contain catalase A but not other peroxisomal enzymes like thiolase. These findings suggest that cells are capable of compensating for overproduced proteins by formation of particular types of structures.

Acetyl-CoA C-Acetyltransferase↗
PubMed1976

Ultrastructural localization of peroxidatic catalase in human peripheral blood leukocytes.

Localization of peroxidatic catalase in human peripheral blood leukocytes was accomplished by the assessment of alkaline diaminobenzidine reaction in the cytoplasmic granules of normal and acatalasemic leukocytes. A modified cytochemical procedure of Novikoff and Goldfischer (Novikoff AB, Goldfischer S: J Histochem Cytochem 17:675, 1969) and of Fahimi (Fahimi HD:J Cell Biol 43:275, 1969) was employed to improve the specificity of alkaline diaminobenzidine test for catalase. Diaminobenzidine-positive reaction for peroxidative catalase was observed in large and medium-sized granules in the cytoplasm of normal neutrophils, but a striking and notable absence of this reaction was observed in acatalasemic neutrophils. The test for myeloperoxidase, with the diaminobenzide reaction performed at neutrality, disclosed positively stained granules in both normal and acatalasemic neutrophils. Similarities in size and configuration of the positively stained granules for these enzymes suggest that catalase is sequestered in organelles which may be primary or azurophilic granules. Myeloperoxidase has been shown to be localized in the primary granules by others. It is possible that catalase and myeloperoxidase may be sequestered together or separately in these granules, but the present data do not permit us to draw this distinction. The ultrastructural localization of peroxidatic catalase and myeloperoxidase has been attempted in eosinophils, lymphocytes, and platelets, and the observations are compared with those of neutrophilic granules. The localization of peroxidatic catalase in monocytes could not be assessed satisfactorily because of the difficulties encountered in proper sampling of these cells.

Acatalasia↗
PubMed1990

Changes in catalase activity in lung and liver after endotoxemia in sheep.

Endotoxemia in the sheep produces oxidant-induced cardiopulmonary dysfunction and lung and liver lipid peroxidation, which can be prevented with exogenous catalase, indicating a role for hydrogen peroxide. We determined whether endotoxin-induced oxidant release altered endogenous catalase activity to help explain the lipid peroxidation. Unanesthetized sheep were given 2 micrograms/kg Escherichia coli endotoxin and killed at 5 hr or 24 hr. Lung and liver lipid peroxidation, measured as malondialdehyde, and catalase activity were determined after endotoxin and compared with controls. Lung tissue MDA increased by 100% at 5 hr and was still elevated by 50% at 24 hr, while catalase activity decreased by 50% at 5 hr and remained decreased, suggesting irreversible inactivation. Liver MDA was also doubled at both 5 and 24 hr, but catalase activity remained unchanged. We conclude that endotoxemia results in a significant inactivation of endogenous catalase activity in lung, but not in liver. The lung may be more prone to a subsequent H2O2 injury before restoration of catalase activity.

Animals↗
PubMed1989

Comparative spectral analysis of mammalian, fungal, and bacterial catalases. Resonance Raman evidence for iron-tyrosinate coordination.

Resonance Raman spectra are reported for catalases from bovine liver, the ascomycete fungus Aspergillus niger, and the bacterium Micrococcus luteus. The vibrational frequencies of the oxidation-, spin-, and coordination number-sensitive spectral bands are indicative of high spin pentacoordinate hemes in the resting ferric enzymes of each of these organisms. This result is in accord with the crystal structure of bovine catalase (Fita, I., and Rossmann, M.G. (1985) J. Mol. Biol. 185, 21-37). In contrast, the crystallographic study of catalase from the ascomycete Penicillium vitale (Vainshtein, B. K., Melik-Adamyan, W. R., Barynin, V. V., Vagin, A.A., Grebenko, A. I., Borisov, V. V., Bartels, K. S., Fita, I., and Rossmann, M. G. (1986) J. Mol. Biol. 188, 49-61) showed electron density on the distal side of the heme which could imply the presence of a sixth ligand, possibly a water molecule. However, both of these crystallographic studies showed the proximal ligand in catalase to be a tyrosine. The present study confirms tyrosinate coordination in each of the three catalases from the appearance of selected resonance-enhanced tyrosine vibrational modes. The most characteristic band is the tyrosinate ring mode at approximately 1612 cm-1 which is maximally enhanced with 488.0 nm excitation. The appearance of tyrosinate modes at 1607 and 1245 cm-1 in the resonance Raman spectra of M. luteus cyano catalase serves to identify tyrosine as an axial ligand in bacterial as well as eukaryotic catalases. Unlike non-heme iron tyrosinate proteins, whose resonance Raman spectra are dominated by several intense bands diagnostic of tyrosine ligation, the heme-linked tyrosine modes are not easily distinguished from the large number of porphyrin vibrations.

Animals↗
PubMedDate not supplied

Effect of superoxide dismutase plus catalase on myocardial infarct size in rabbits.

A previous study by the authors showed that myocardial infarct size in the rabbit, measured after 45 mins of ischemia and 3 h of reperfusion, could be limited by administration of superoxide dismutase (SOD) plus catalase. The present study examined whether this infarct size limitation is sustained for the following three days. Under anesthesia, a coronary branch of the Japanese white rabbit was occluded for 45 mins and then reperfused. Three days after surgery, the heart was excised and the volume of myocardium supplied by the occluded coronary branch (ischemic zone size) was assessed with fluorescent particles and the infarct size was estimated by hematoxylin and eosin and with Mallory's staining. The SOD plus catalase group (n = 14) received 15,000 units/kg of SOD plus 50,000 units/kg of catalase in saline over 90 mins, starting 15 mins before the coronary occlusion. Saline was infused in the control group (n = 15). Three rabbits in the control group and three in the SOD plus catalase group died of ventricular fibrillation during the ischemic period. Three control and two SOD plus catalase rabbits were excluded because the ischemic zone was ambiguous. The percentage of the ischemic zone which was infarcted was 59.4 +/- 6.9% (mean +/- SE) in the control group (n = 9) and 49.4 +/- 5.1% in the SOD plus catalase group (n = 9). These were not statistically different. Ischemic zone size and hemodynamic parameters were similar in the two groups. These findings suggest that SOD plus catalase may serve only to delay rather than prevent myocardial infarction.

Animals↗