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

The effect of atmospheric oxygen on the viability of 13 strains of anaerobic bacteria, two strains of facultative bacteria, and one aerobic organism was examined. There were great variations in oxygen tolerance among the bacteria. All facultative bacteria survived more than 72 h of exposure to atmospheric oxygen. The survival time for anaerobes ranged from less than 45 min for Peptostreptococcus anaerobius to more than 72 h for two Clostridium perfringens strains. An effort was made to relate the degree of oxygen tolerance to the activities of superoxide dismutase, catalase, and peroxidases in cell-free extracts of the bacteria. All facultative bacteria and a number of anaerobic bacteria possessed superoxide dismutase. There was a correlation between superoxide dismutase activity and oxygen tolerance, but there were notable exceptions. Polyacrylamide gel electropherograms stained for superoxide dismutase indicated that many of the anaerobic bacteria contained at least two electrophoretically distinct enzymes with superoxide dismutase activity. All facultative bacteria contained peroxidase, whereas none of the anaerobic bacteria possessed measurable amounts of this enzyme. Catalase activity was variable among the bacteria and showed no relationship to oxygen tolerance. The ability of the bacteria to reduce oxygen was also examined and related to enzyme content and oxygen tolerance. In general, organisms that survived for relatively long periods of time in the presence of oxygen but demonstrated little superoxide dismutase activity reduced little oxygen. The effects of medium composition and conditions of growth were examined for their influence on the level of the three enzymes. Bacteria grown on the surface of an enriched blood agar medium generally had more enzyme activity than bacteria grown in a liquid medium. The data indicate that superoxide dismutase activity and oxygen reduction rates are important determinants related to the tolerance of anaerobic bacteria to oxygen.
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PMID:Factors related to the oxygen tolerance of anaerobic bacteria. 69 63

The tumor promoter phorbol-12-myristate-13-acetate (PMA) increases the poly ADP-ribosylation of acid extractable (0.2N H2SO4) nuclear proteins in mouse embryo fibroblasts C3H10T1/2. Catalase suppresses the reaction by approximately 50%. Polyacrylamide gel electrophoresis reveals that the core histones H2B, A24 and H3d serve as major poly ADP-ribose acceptors. Smaller amounts of poly ADP-ribose are associated with histones H2A/H3 and H1. Poly ADP-ribosylation of histones may change the nucleosomal structure and function and play a role in PMA induced modulation of gene expression in promotion.
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PMID:Poly ADP-ribosylation of histones in tumor promoter phorbol-12-myristate-13-acetate treated mouse embryo fibroblasts C3H10T1/2. 406 47

Streptomyces coelicolor ATCC 10147 produced catalases whose electrophoretic mobility varied depending on the growth phase in liquid culture. Polyacrylamide gel electrophoresis of cell extracts resulted in six catalase activity bands, which were designated Cat1 to Ca6. Of these, Cat4 appeared during all growth phases, whereas Cat1 appeared only during the stationary phase. Catalase-deficient mutants were screened by the H2O2 bubbling test following NTG mutagenesis. In all the non-bubbling mutants tested, the Cat4 activity band significantly decreased or disappeared, suggesting that Cat4 is the major catalase. Cat4 was purified to electrophoretic homogeneity and some of its properties analysed. The enzyme has a native molecular mass of 225 kDa, as determined by gel permeation column chromatography, and consists of four identical subunits of 57 kDa, as determined by SDS-PAGE. The enzyme contains 2.6 molecules of protohaem IX per tetramer, as indicated by the absorption spectrum. It was not reducible by sodium dithionite and exhibited no peroxidase activity with o-dianisidine as the substrate. All these characteristics, as well as inhibitor studies, indicate that the major vegetative catalase in S. coelicolor, unlike E. coli vegetative catalase, is a member of the typical monofunctional catalases found in eukaryotes and some bacteria.
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PMID:Characterization of the major catalase from Streptomyces coelicolor ATCC 10147. 788 56

We studied the effects of moist chilling and warming on storage protein mobilization in walnut (Juglans regia L.) kernels to assess the metabolic inhibition theory, which states that dormant seeds are unable to utilize their own food reserves and that cold conditions allow germination by activating hydrolases involved in reserve mobilization. Stratifying kernels at 5 degrees C for 40 days enhanced their germination. During both cold stratification and warm incubation of kernels, storage protein mobilization occurred in cotyledons rather than axes. Kernel amino acid concentration increased during protein mobilization, with axes of warm-incubated kernels having particularly high amino acid concentrations. Polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate (SDS-PAGE) of the soluble protein fractions from both cold-stratified and warm-incubated cotyledons revealed increased band intensities of putative glutelins (19-22 and 32-35 kDa). A very high molecular weight protease was detected by gelatin SDS-PAGE that was most active at acid to neutral pHs in imbibed, cold stratified and germinated kernels suggesting the protease(s) was synthesized earlier in the mature seeds. Thus, in dormant walnut kernels there is no block to protein mobilization, and imbibition alone is sufficient to initiate proteolysis. Catalase activity was higher in warm-incubated kernels than in cold-stratified kernels, suggesting that seed aging is hastened under warm conditions and that cold stratification in walnut kernels might involve activation of cellular repair mechanisms.
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PMID:Alleviation of dormancy in walnut kernels by moist chilling is independent from storage protein mobilization. 1724 94