Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P04040 (Catalase)
 3,577 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The crude homogenate of cells from Chlamydomonas reinhardii was placed on a linear gradient from 30% to 60% sucrose and centrifuged for 4 hours at 60 000 g. After fractionation of the gradient the distribution of enzymes was determined. Hydroxypyruvate reductase and glycolate dehydrogenase, two markers for peroxisomes, appeared with one sharp peak at density 1.185 g/cm(3) within the gradient. Twenty-five percent of the hydroxypyruvate reductase was particulate and 75% was found as solubles in the top fractions. The peaks of both enzymes matched exactly the peak of the cytochrome oxidase which is a marker for mitochondria. The profile for malate dehydrogenase was the same as that for hydroxypyruvate reductase. Catalase, however, showed two peaks. One coincided with the peak of cytochrome oxidase and the other appeared at density 1.22 g/cm(3). More than 50% of the catalase moved into the gradient during centrifugation.
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PMID:[Distribution of microbody enzymes from Chlamydomonas on sucrose gradients]. 2444 97

When the sections of the spadix appendix of Arum are incubated in a medium containing diaminobenzidine and H2O2, only the membrane of microbodies is stained. On the other hand, microbodies of Sauromatum show a stained matrix as usual. Catalase-containing cell organelles isolated from spadix appendices of Arum show the same typical membrane staining as the microbodies in situ do. Thus the identity of these organelles with microbodies seems to be proved. After anthesis the microbodies in situ usually do not give a positive reaction for catalase with diaminobenzidine and H2O2. However, cytochemical and biochemical tests for catalase on microbodies isolated during this stage of development clearly demonstrate the presence of this enzyme. Uricase is localized in the microbodies of Arum as well as catalase. No malate dehydrogenase, peroxidase, and allantoinase could be found in the microbodies. Before anthesis the microbodies of spadix appendices of Arum have an equilibrium density in aqueous sucrose of 1.22 gcm(-3). After anthesis the density changes into 1.23 to 1.24 gcm(-3).
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PMID:[Studies on microbodies in spadix appendices of Arum maculatum L. and Sauromatum guttatum schott]. 2449 39

Aspergillus flavus infection is a major issue for safe food storage. In this study, we constructed an efficient prokaryotic expression system for puroindoline B (PINB) protein to detect its antifungal activity. The Puroindoline b gene was cloned into pET-28a (+) vector and expressed in Escherichia coli. Treatment with fusion PINB revealed that it inhibits mycelial growth of A. flavus, a common grain mold. Moreover, fusion PINB-treated A. flavus mycelium withered and exhibited a sunken spore head. As fusion PINB concentration increased, electrical conductivity in mycelium also increased, indicative of cell membrane damage. Furthermore, intracellular malate dehydrogenase and succinate dehydrogenase activity decreased, revealing a disruption in the tricarboxylic acid cycle. Moreover, the dampened activity of the ion pump Na+K+-ATPase negatively affected the intracellular regulation of both ions. Catalase and superoxide dismutase activity decreased, thus reducing antioxidant capacity, a result confirmed with an increase in malondialdehyde content. Changes to the GSH/GSSG ratio indicated a shift to an intracellular oxidative state. At the same time, laser scanning confocal microscopy assay showed the accumulation of reactive oxygen species and nuclear damage. Therefore, the PINB fusion protein may have the potential to control A. flavus in grain storage and food preservation.
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PMID:Antifungal Effects of Fusion Puroindoline B on the Surface and Intracellular Environment of Aspergillus flavus. 3248 75

Colloidal suspensions of silver nanoparticles (AgNPs) with surface modified by capping with citrate ions were synthesized by chemical reduction method. Transmission and Scanning Electron Microscopy as well as darkfield Optical Microscopy provided information on the nanoparticle morphology, with fine symmetrical grains and log-normal fitted size distribution. Small Angle X-ray Scattering method allowed theoretical confirmation of colloidal silver nanoparticle fine granularity, based on measurements in the native fluid sample. UV-Vis spectrophotometry allowed studying the Localized Surface Plasmon Resonance band versus the stability of the citrate-AgNP sample after storage and after UV-C exposure. The colloidal AgNP impact on Phanerochaete chrysosporium environmental microorganisms was studied by specific biochemical investigations. Silver released from the colloidal suspension of AgNPs was supposed to induce changes in some antioxidant enzymes and in some enzymes of Krebs' cycle. Catalase activity was moderately changed (an increase with over 50%) as well as superoxide dismutase activity, while the diminution of the activities of four dehydrogenases synthesized in the fungus mycelium was emphasized also: a decrease with about 60% for malate dehydrogenase, with over 50% for isocitrate dehydrogenase and succinate dehydrogenase and with about 40% for alpha-ketoglutarate dehydrogenase. These findings suggested the nano-toxicological issues of citrate-AgNPs impact on the environmental beneficial microorganisms.
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PMID:Citrate-silver nanoparticles and their impact on some environmental beneficial fungi. 3330 44


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