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Query: UNIPROT:P04040 (Catalase)
 3,577 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The influence on diaminobenzidine staining of four variables: prefixation in aldehyde, temperature and pH of incubation, and H2O2 concentration, was investigated in catalase-, as well as in peroxydase-containing material. Catalase from five different sources and five types of peroxidase were examined. It is concluded: (a) when cells are incubated without prior fixation, in a DAB medium at room temperature and pH 7.3 with 0.003% H2O2, peroxidases produce a visible cytochemical stain, while catalases do not; (b) the cytochemical reaction elicited by catalases is stimulated by prior aldehyde fixation in specified conditions, and incubation at 45 degrees C and pH 9.7 with 0.06% H2O2; (c) under the latter circumstances several peroxidases also stain. Ultrastructural preservation is satisfactory in tissues incubated prior to fixation.
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PMID:Cytochemical discrimination between catalases and peroxidases using diaminobenzidine. 23 53

The DAB reactivity of the midintestine of the earthworm, consisting of epithelial layer, muscle layer, and chloragogen tissue, was examined electron microscopically. Besides the mitochondrial membranes of the examined cell types and the hemoglobin content of the blood vessels and chloragogen cells, a considerable DAB reactivity was found in the whole cytosol of the chloragocytes. The DAB reaction of the cytosol was more intensive when incubation medium for catalase, less intensive when incubation medium for peroxidase, was used and did not occur when H2O2 was omitted. Cytosol of the chloragogen cells was isolated and preliminary assay of catalase and peroxidase activities was made. Cytosol samples showed moderate peroxidase activity, but catalase activity measured by the decomposition of hydrogen peroxide showed a very high rate. Catalase and peroxidase activities of the cytosol were heat-sensitive and might have been inhibited by azide and cyanide, respectively. Results prove the assumption that the intensive DAB reactivity of the chloragocyte cytosol is caused by its extraperoxisomal catalase content.
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PMID:Evidence of the presence of extraperoxisomal catalase in chloragogen cells of the earthworm, Lumbricus terrestris L. 66 91

The distribution of microperoxisomes was studied in areas of the central nervous system having high concentrations of catecholaminergic neurons and in areas lacking this neuron type, using the alkaline DAB cytochemical method for catalase. Substantial numbers of microperoxisomes are found in neurons in the locus coeruleus and in nucleus A1 of the medulla, as well as in the substantia nigra, whereas few catalase-reactive bodies are seen in neurons of the cerebrum and cerebellum. The number of catalase-reactive microperoxisomes per unit area in the catecholaminergic neurons of the CNS is comparable to the number seen previously in neurons of the peripheral cervical sympathetic ganglia. Some spinal cord neurons also contain reactive microperoxisomes. Catalase-reactive microperoxisomes are numerous in oligodendrocytes of all areas studied, and in ependymal cells bordering the third and fourth ventricles. Astrocytes contain few reactive structures in the cytoplasm near the nucleus, but they are readily found in astrocytic processes and end-feet.
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PMID:Microperoxisome distribution in the central nervous system of the rat. 99 Sep 13

This investigation was undertaken to study the ontogeny of hepatic, renal, and intestinal peroxisomes and/or microperoxisomes during thyroxine-induced anuran metamorphosis. Catalase activity was localized cytochemically after incubation in DAB medium, and studied biochemically by a spectrophotometric method. Our morphological and biochemical investigations suggest the formation of a new population of peroxisomes during the hormonal treatment. This is obvious especially for microperoxisomes of the intestinal epithelium since the larval tissue is completely replaced by a new layer during thyroxine-induced metamorphosis. For the peroxisomes of hepatocytes and kidney proximal tubule cells, our assumption is based on the following observations: 1) The number of peroxisomes increases in liver and kidney during thyroxine treatment; 2) this proliferation is accompanied by an enlargement of renal peroxisomes; and 3) 16 days after the beginning of the hormonal treatment, 5.4- and 2.4-fold increases are found for the specific activities of hepatic and renal catalase, respectively. A temporal coordination exists between the structure and the metabolism of peroxisomes and mitochondria during thyroxine-induced metamorphosis.
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PMID:Development of peroxisomes in amphibians. III. Study on liver, kidney, and intestine during thyroxine-induced metamorphosis. 660 16

The ontogeny of catalase-containing organelles was studied by cytochemical and biochemical methods in the liver, kidney, and pancreas during the development of Rana catesbeiana. The biochemical differentiation of peroxisome in the liver and kidney was compared to that of Xenopus laevis. Catalase activity was localized after incubation in DAB medium and studied biochemically by a spectrophotometric method. In Rana Catesbeiana the number of catalase-positive organelles per cell section is low in all three organs during premetamorphosis; their number increases substantially in the liver and kidney of froglets, while it remains almost stable in the pancreas. No further increase is observed in the adult. Biochemically, the liver, kidney, and pancreas of tadpoles exhibit, respectively, 12,22 and 63% of the catalase activity found in the adult tissues. After metamorphosis an important increase of catalase activity is particularly noted in liver and kidney, the activity being, respectively, 43 and 77% of that of adult bullfrogs. On the other hand, no change in catalase activity in the liver and kidney is noted during the entire development of Xenopus laevis. The present study illustrates the very different developmental pattern of catalase activity observed during the development of two anuran amphibians. The different development pattern of the same enzyme within the small intestine, liver, kidney, and pancreas in Rana catesbeiana is also stressed.
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PMID:Development of peroxisomes in amphibians. II. Cytochemical and biochemical studies on the liver, kidney, and pancreas. 698 9

The ultrastructure of mesophyll cells from leaves of a catalase-deficient homozygous mutant of barley (RPr 79/4), which grows poorly in air but normally in carbon-dioxide-enriched air, has been examined and compared with that of the cultivar Maris Mink with normal catalase levels, and with that of the F1 progeny of the cross RPr 79/4xGolden Promise with 50% normal catalase levels. In Maris Mink, the F1 progeny, and the mutant in which photorespiration had been suppressed by growing in air enriched to 0.2% CO2, the ultrastructure of the mesophyll cells was typical of young festucoid leaves with the peroxisomes containing thread-like inclusions. In air-grown leaves of the mutant RPr 79/4 which had developed lesions and become shrivelled, all the chloroplasts were irregular in outline, and in some the granal membranes were disrupted into abnormal honeycomb configurations and the plastid envelope was absent. In necrotic tissue, membrane fragments and osmiophilic droplets marked the sites of severely damaged chloroplasts. The peroxisomes contained diffuse tufts of electron-opaque material as well as fibrous strands. Catalase activity, visualised cytochemically by DAB, was located exclusively in the peroxisomes of Maris Mink and the F1 progeny, but none was found in the mutant grown either in CO2-rich air, or in normal air. The role of catalase in preventing ultrastructural damage by hydrogen peroxide during photorespiration is discussed.
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PMID:Ultrastructure of the mesophyll cells of leaves of a catalase-deficient mutant of barley (Hordeum vulgare L.). 2425 27

Catalase is an iron porphyrin enzyme, which serves as an efficient scavenger of reactive oxygen species (ROS) to avoid oxidative damage. In sugarcane, the enzymatic activity of catalase in a variety (Yacheng05-179) resistant to the smut pathogen Sporisorium scitamineum was always higher than that of the susceptible variety (Liucheng03-182), suggesting that catalase activity may have a positive correlation with smut resistance in sugarcane. To understand the function of catalase at the molecular level, a cDNA sequence of ScCAT1 (GenBank Accession No. KF664183), was isolated from sugarcane infected by S. scitamineum. ScCAT1 was predicted to encode 492 amino acid residues, and its deduced amino acid sequence shared a high degree of homology with other plant catalases. Enhanced growth of ScCAT1 in recombinant Escherichia coli Rosetta cells under the stresses of CuCl2, CdCl2 and NaCl indicated its high tolerance. Q-PCR results showed that ScCAT1 was expressed at relatively high levels in the bud, whereas expression was moderate in stem epidermis and stem pith. Different kinds of stresses, including S. scitamineum challenge, plant hormones (SA, MeJA and ABA) treatments, oxidative (H2O2) stress, heavy metal (CuCl2) and hyper-osmotic (PEG and NaCl) stresses, triggered a significant induction of ScCAT1. The ScCAT1 protein appeared to localize in plasma membrane and cytoplasm. Furthermore, histochemical assays using DAB and trypan blue staining, as well as conductivity measurement, indicated that ScCAT1 may confer the sugarcane immunity. In conclusion, the positive response of ScCAT1 to biotic and abiotic stresses suggests that ScCAT1 is involved in protection of sugarcane against reactive oxidant-related environmental stimuli.
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PMID:Isolation of a novel peroxisomal catalase gene from sugarcane, which is responsive to biotic and abiotic stresses. 2439 35

Biotic stress, as a result of plant-pathogen interactions, induces the accumulation of reactive oxygen species in the cells, causing severe oxidative damage to plants and pathogens. To overcome this damage, both the host and pathogen have developed antioxidant systems to quench excess ROS and keep ROS production and scavenging systems under control. Data on ROS-scavenging systems in the necrotrophic plant pathogen Rhizoctonia solani are just emerging. We formerly identified vitamin B6 biosynthetic machinery of R. solani AG3 as a powerful antioxidant exhibiting a high ability to quench ROS, similar to CATALASE (CAT) and GLUTATHIONE S-TRANSFERASE (GST). Here, we provide evidence on the involvement of R. solani vitamin B6 biosynthetic pathway genes; RsolPDX1 (KF620111.1), RsolPDX2 (KF620112.1), and RsolPLR (KJ395592.1) in vitamin B6 de novo biosynthesis by yeast complementation assays. Since gene expression studies focusing on oxidative stress responses of both the plant and the pathogen following R. solani infection are very limited, this study is the first coexpression analysis of genes encoding vitamin B6, CAT and GST in plant and fungal tissues of three pathosystems during interaction of different AG groups of R. solani with their respective hosts. The findings indicate that distinct expression patterns of fungal and host antioxidant genes were correlated in necrotic tissues and their surrounding areas in each of the three R. solani pathosystems: potato sprout-R. solani AG3; soybean hypocotyl-R. solani AG4 and soybean leaves-R. solani AG1-IA interactions. Levels of ROS increased in all types of potato and soybean tissues, and in fungal hyphae following infection of R. solani AGs as determined by non-fluorescence and fluorescence methods using H2DCF-DA and DAB, respectively. Overall, we demonstrate that the co-expression and accumulation of certain plant and pathogen ROS-antioxidant related genes in each pathosystem are highlighted and might be critical during disease development from the plant's point of view, and in pathogenicity and developing of infection structures from the fungal point of view.
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PMID:Antioxidant genes of plants and fungal pathogens are distinctly regulated during disease development in different Rhizoctonia solani pathosystems. 2946 4