Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.4.25.1 (proteasome)
28,817 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The influence of culture medium composition on alkaline protease production was studies. Various carbon sources such as glycerol, glucose, lactose and starch were tested. Different concentrations of lactose and bactopeptone have been tested. The optimum medium composition was found to be: (g/l) lactose 20.0; bactopeptne Difco 10.0; NaCl 1.5;mgSO47.H20 0.15; CaCl2 0.06; K2HPO4 1.5; KH2PO4 1.5; Na2SO4 1.5; MnCL2.4H2O 0.01. A cell concentration of c.a 9.5 g/l has been obtained after 30 hours. The maximun alkaline protease production (5,000 uAPAM/ml) was attained after 60 hours. The trials were carried on rotary shaker in 1 liter erlenmeyer flasks containing 250 ml of medium.
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PMID:[Alkaline protease production]. 81 79

The effect of glucose and amino acids on the synthesis of alkaline protease of the prototroph strain and auxotrophs of Bacillus subtilis A-50 was studied. There are both general and different from one another mechanisms of regulation for sporulation and protease synthesis as one of early stages of sporulation. Most auxotroph mutations pleiotropically decrease the level of protease synthesis and the efficiency of sporulation. At the same time the differences depending on sporulation and protease formation from glucose, amino acids and caseinoacids are observed. The increase in glucose concentration in the medium from 0.5 to 5% leads to intensification of protease synthesis and decrease of the sporulation efficiency. The suppression of alkaline protease formation in B. subtilis occurs when amino acid concentration is of the order of 1.5 mg/ml in the studied combination in the presence of 1--5% glucose. The strongest inhibitory effect was discovered for 2d, 3d and 4th amino acid groups in the presence of 5% glucose, whereas amino acids of the first group stimulate the protease synthesis in the presence of 2% glucose. The stimulatory effect of amino acids of the first groups is due to histidine and arginine.
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PMID:[Regulation of alkaline protease synthesis in Bacillus subtilis A-50]. 81 33

Glur mutants of Bacillus subtilis A-50 capable of sporulating in the medium containing 5% glucose are isolated. The mutants are divided into three groups. The first group comprises glur mutants whose level of proteolytic activity is lower than that of the initial strain A-50. The productivity of mutants of the 2nd group is equal to the level of alkaline proteinase synthesis characteristics of the original strain. In mutants of the third group the level of alkaline protease synthesis exceeds the productivity of the initial strain. There was no correlation between the efficiency of spore formation in the mutants obtained and the level of alkaline protease activity. The mutants of different groups differ in their ability to grow on different sugars.
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PMID:[Mutants of Bacillus subtilis--producer of alkaline proteinase, sporulating in the presence of high concentrations of glucose]. 82 55

For a relaxed (rel-), protease producing (A-type) and a stringent (rel+), not-protease producing (B-type) variant of Bacillus licheniformis we determined fermentation patterns and products, growth parameters and alkaline protease-production (if any) in anaerobic, glucose-grown chemostats and batch-cultures. Glucose is dissimilated via glycolysis and oxidative pentose phosphate pathway simultaneously; the relative share of these two routes depends on growth phase (in batch) and specific growth rate (in chemostat). Predominant products are lactate, glycerol and acetaldehyde for A-type batches and acetaldehyde, ethanol, acetate and lactate for B-type batches. Both types show a considerable acetaldehyde production. In chemostat cultures, the fermentation products resemble those in batch-culture. From the anaerobic batches and chemostats, we conclude that the A-type (with low ATP-yield) will have a YATPmax of probably 12.9 g/mol and the B-type (with high ATP-yield) a YATPmax of about 10.1 g/mol. For batch-cultures, both types have about the same, high Yglucose (12 g/mol). So, the slow-growing A-type has a relatively high efficiency of anaerobic growth (i.e. an efficient use of ATP) and the fast-growing B-type a relatively low efficiency of anaerobic growth. In aerobic batch-cultures, we found 48, respectively 41% glucose-carbon conversion into mainly glycerol and pyruvate, respectively acetate as overflow metabolites in the A- and B-type. In both aerobic and anaerobic batch-cultures of the A-type, protease is produced predominantly in the logarithmic and early stationary phase, while a low but steady production is maintained in the stationary phase. Protease production occurs via de novo synthesis; up to 10% of the total protease in a culture is present in a cell-associated form. Although anaerobic protease production (expressed as protease per amount of biomass) is much higher than for aerobic conditions, specific rates of production are in the same range as for aerobic conditions while, most important, the substrate costs of anaerobic production are very much higher than for aerobic conditions.
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PMID:Formation of fermentation products and extracellular protease during anaerobic growth of Bacillus licheniformis in chemostat and batch-culture. 180 2

We have investigated the effect of elastase and alkaline protease from Pseudomonas aeruginosa on airway secretion into the trachea of anesthetized cats and from human bronchial mucosa in vitro. Secretory macromolecules were radiolabeled biosynthetically with two precursors in the cat, [3H]glucose and [35S]sulfate, and with [35S]-sulfate only in human tissue. Both enzymes (2.6 x 10(-9) to 1.3 x 10(-6)M elastase and 8 x 10(-9) to 2.4 x 10(-6)M alkaline protease) released radiolabeled macromolecules in a concentration-dependent manner from the two preparations. Purified elastase, 1.3 x 10(-6)M, released radiolabeled macromolecules (delta 3H = +397 +/- 72%, delta 35S 225 +/- 40% over control, P less than 0.001) and periodic acid-Schiff- (PAS) reactive glycoconjugates (delta PAS = +4.1 +/- 0.96 micrograms/min or +102 +/- 20%; P less than 0.01) from cat trachea, as did alkaline protease, 2.4 x 10(-6)M (delta 3H = +356 +/- 57%, delta 35S = +176 +/- 25%, delta PAS = +7.5 +/- 1.3 micrograms/min or 194 +/- 36%, P less than 0.001). Increases in 3H exceeded those of 35S, suggesting surface epithelium as the main source of secretion. Inhibition of enzyme activity abolished secretory effects. Both enzymes also stimulated secretion from human bronchus (e.g., with elastase, 1.3 x 10(-6)M: delta 35S = +331 +/- 67%, delta PAS = +4.3 +/- 0.92 micrograms/min or +131 +/- 24%, P less than 0.001; with alkaline protease, 2.4 x 10(-6)M: delta 35S = +220 +/- 67%, delta PAS = +12.7 +/- 3.2 micrograms/min or +575 +/- 245%, P less than 0.001).(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Stimulation of secretion into human and feline airways by Pseudomonas aeruginosa proteases. 190 6

1. NAD(P)ase activity was stimulated when 1% sorbose was present in the culture medium of A. nidulans, and this effect was partially reversed by 1% glucose. 2. The level of extracellular NAD(P)ase was more affected by sorbose in the culture medium than the intracellular enzyme and no morphological changes were obtained. 3. The sorbose effect on NAD(P)ase activity appears to be specific since two other exoenzymes tested (beta-glucosidase and alkaline protease) show normal secretion patterns. 4. These findings suggest that the sorbose effect on NAD(P)ase production may be the consequence of metabolic disorders not necessarily linked with the morphological changes induced by the ketohexose.
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PMID:The effect of sorbose on NAD(P)ase production by Aspergillus nidulans. 285 39

Flagellate bacteria can respond to a wide range of environmental chemicals and a variety of physical parameters, and integrate those responses. The most important thing for a cell is to maintain its energy level; bacteria therefore respond directly to any changes in their PMF. This has been likened to higher organisms responding to a physiological change, for example, a fall in blood glucose. In addition, if the PMF is high, the cell is free to respond to a limited range of metabolites and possibly move to an area that will allow an increased growth rate. Bacteria do not sense all amino acids, as the space available on the cytoplasmic membrane is limited, and a change in a few important metabolites is probably a good measure of the general environment around the cell. The sensory response does not require either transport into the cell or metabolism of the chemical, only the binding to the specific MCP. The cell could have a mutation in the pathway metabolizing the chemoeffector, but it would still respond to changes in the concentration of that compound. This taken with the ability of the cells to adapt to the stimulus has been considered to be the prokaryotic equivalent of smell and taste.
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PMID:Sensory transduction in flagellate bacteria. 332 83

The activities of some antioxidative and hexose monophosphate shunt enzymes, as well as of 2 hydrolases were studied in skeletal muscle biopsy specimens taken from 39 patients with neuromuscular diseases and from 15 controls. The activity of Se-dependent glutathione peroxidase was higher in patients with congenital myotonia, whereas in the other diagnostic groups this enzyme activity was the same as in the controls. The Se-independent and total glutathione peroxidase activity of patients in the various diagnostic groups did not differ from the controls. Moreover, no difference were observed in catalase activity between the patient groups and the controls. The activities of the rate limiting enzymes of hexose monophosphate shunt, glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase of muscle biopsy samples of various patient groups did not show any significant difference from controls. The activity of a lysosomal hydrolase, beta-N-acetylglucosaminidase, was increased in patients with polyneuropathy and the activity of a nonlysosomal protease, alkaline protease, was high in patients with Charcot-Marie-Tooth disease. The activities of Se-dependent glutathione peroxidase, 6-phosphogluconate dehydrogenase and of both hydrolases showed a significant correlation to the magnitude of muscle atrophy.
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PMID:Activities of some antioxidative and hexose monophosphate shunt enzymes of skeletal muscle in neuromuscular diseases. 353 84

Using reversed-phase high-performance liquid chromatography (HPLC) it was possible to isolate 32P-labelled active-site regions of various proteins from the bacterial phosphoenolpyruvate-dependent phosphotransferase system. The purified peptides obtained by proteolytic cleavage with Lys-C protease and trypsin were sequenced by the gas phase method. The fragments derived from enzyme I (MW 70 000) of two streptococcal species show 100% homology. The analogous peptide of Staphylococcus aureus Enzyme I differs in the N-terminal region. A labelled peptide from the glucose-specific enzyme III protein of Escherichia coli obtained by cleavage with alkaline protease was isolated and sequenced. It could be fitted into the primary structure of this protein, which was derived from DNA sequence data. The active-site histidine residue of this protein is therefore localized at position 91. The HPLC separation method described is suitable for the isolation of peptides derived from active sites containing labile amino acid derivatives such as phosphohistidines.
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PMID:The bacterial phosphoenolpyruvate-dependent phosphotransferase system. Isolation of active site peptides by reversed-phase high-performance liquid chromatography and determination of their primary structure. 392 66

An intensive parasexual genetics program in which industrial strains of Penicillium chrysogenum were used culminated in the isolation of a number of heterozygous diploid strains. The diploid clones were selected from heterokaryons formed from matings between mutant strains having complementary biochemical and conidial color markers. Several diploid cultures were compared with their haploid wild-type parents and other distantly related production strains on the basis of a variety of cultural and physiological criteria. The diploid strains characteristically produced conidia of larger volume and higher deoxyribonucleic acid content. Some were vigorous with respect to growth rate and onset and degree of conidiation. One diploid strain (WC-9) had a 46% greater oxygen uptake rate and oxidized glucose at a 57% greater rate than its haploid parent (M-2). It also produced 33% higher concentrations of beta-galactosidase, 66% more alkaline protease, and 53% more glucose oxidase than the M-2 haploid parent. The selection of rare stable diploid mold cultures through the use of parasexual genetics offers a unique approach to the direct selection of mutants with potential for increased enzyme formation.
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PMID:Biochemical properties of haploid and diploid strains of Penicillium chrysogenum. 511 5


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