Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.17 (lysozyme)
 21,489 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Pseudomonas aeruginosa PAO1 released a significant amount of a cytoplasmic enzyme, glucose-6-phosphate dehydrogenase, in the presence of aminoglycoside and lysozyme. The extent of the enzyme release was inversely related to the MICs of the aminoglycoside. However, the aminoglycoside-resistant strain F3721, treated in the same way; released a less enzyme. The F3721 LPS was extracted in the phenol phase instead of the water phase in which PAO1 LPS was easily extracted. Electrophoretic analysis of the F3721 LPS showed the ladder bands at the high Mr position, suggesting that the LPS of the aminoglycoside-resistant cells has a structural modification(s) which somehow protects the outer membrane from aminoglycoside-mediated damage.
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PMID:Aminoglycoside resistance in Pseudomonas aeruginosa due to outer membrane stabilization. 179 Jul 21

We have developed a technique which utilizes matrix-assisted laser desorption mass spectrometry to study the subunit association of proteins. Aqueous protein samples are treated with a dilute solution of glutaraldehyde, a cross-linking agent which reacts with free amino groups on proteins. This agent effectively traps the multimeric form, preventing it from dissociating in the sample preparation and desorption process. Proteins measured include lysozyme, carbonic anhydrase, apomyoglobin, glucose 6-phosphate dehydrogenase, ovine lutropin, yeast alcohol dehydrogenase, avidin and pyruvate kinase. Dimeric and tetrameric complexes up to 250,000 Da have been measured in this manner.
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PMID:Assessing the multimeric states of proteins: studies using laser desorption mass spectrometry. 181 90

The catalytic activities of lysozyme, horseradish peroxidase (HP), catalase, glucose-6-phosphate dehydrogenase (G6PDH) and lactate dehydrogenase (LDH) were studied in aqueous solutions and after isolation of the enzymes from mixed reversed micelles of Aerosol OT and Triton X-45 by organic solvents (acetone, ethanol, isopropanol), by acetone-water mixtures, as well as by aqueous solutions containing urea, glycerol, polyethylene glycol 6000 and ammonium sulphate. The isolation conditions were found for catalase with retaining all the activity and for HP and lysozyme with retaining 72 and 84% of the catalytic activity, respectively. The G6PDH isolation from micelles by aqueous solutions of urea (6%) and glycerol (10%) resulted in retaining only 43% of the enzyme activity and led to almost complete inactivation of LDH. Stability of the enzymes after their entrapment in micelles and isolation from those is compared with thermostability of the same enzymes in aqueous solutions.
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PMID:[Isolation of enzymes from mixed reversed micelles of surface-active agents]. 245 51

The localization of anhydrotetracycline oxygenase and glucose-6-phosphate dehydrogenase (EC 1.1.1.49) was studied by determining the enzyme activities in subcellular fractions obtained by differential centrifugation of the mycelia of Streptomyces aureofaciens after lysozyme treatment. Glucose-6-phosphate dehydrogenase was a typical cytoplasmic enzyme both in the low- and high-production strain. Anhydrotetracycline oxygenase was found in the membrane fraction of the low-production strain. In the high-production strain, it was detected in several fractions, the highest activity being found in cytoplasm. The presence of 10 microM benzyl thiocyanate in the culture medium significantly changed the distribution of the latter enzyme in both strains. The redistribution of the enzymes is discussed with respect to tetracycline over-production.
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PMID:Subcellular localization of enzymes in Streptomyces aureofaciens and its alteration by benzyl thiocyanate. II. Anhydrotetracycline oxygenase and glucose-6-phosphate dehydrogenase. 312 78

In a controlled study the activity of glucose-6-phosphate dehydrogenase (G-6-PD) in red and white blood cells, gamma-glutamyl transpeptidase (gamma-GT) and lysozyme in serum and white blood cells was studied in 22 drug-free schizophrenic patients and 17 healthy volunteers. The activities of the above enzymes were found to be reduced in the white cells of schizophrenics compared with controls. The differences in activity of G-6-PD in red cells and of gamma-GT and lysozyme in serum between the two groups were not revealed as significant. The observed low enzyme activities might provide a further basis for interpreting the reported functional deficiency in neutrophils of schizophrenics. Possible mechanisms in relation to biological abnormalities in schizophrenia are discussed.
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PMID:Enzyme activity of G-6-PD, gamma-GT and lysozyme in white cells of schizophrenics. 610 36

The localization of the Pseudomonas aeruginosa lectins (PA-I and PA-II) was studied using methods of osmotic shock, freezing and thawing and spheroplast formation. Very slight release of the two lectins occurred when P. aeruginosa was exposed to magnesium-osmotic shock or was frozen and thawed. Under these conditions, release of the periplasmic 5'-nucleotidase occurred, whereas no release of cytoplasmic glucose-6-phosphate dehydrogenase activity was detected. Formation of spheroplasts from P. aeruginosa by gradual removal of the bacterial envelopes revealed low lectin activity in the treatment fluids. Osmotic shock treatment of the lysozyme treated mureinoplasts resulted in low release of glucose-6-phosphate dehydrogenase and the two lectins (10-13%) and a considerable activity (38.4%) of 5'-nucleotidase. The presence of the lectins on the outer and the cytoplasmic membranes enabled intact cells and spheroplasts of P. aeruginosa to agglutinate papain-treated human erythrocytes. These results indicate that the two lectins are located mainly in the cytoplasm with small fractions on the cytoplasmic and outer membranes and in the periplasmic space.
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PMID:The intracellular localization of Pseudomonas aeruginosa lectins. 631 95

A micromethod is described for the production of lysed preparations of Thiobacillus A2 following treatment with lysozyme and EDTA. These may be used for the assay of intra-cellular enzymes including rhodanese, hexokinase, glucose 6-phosphate dehydrogenase and phosphoglucoseisomerase. The procedure is useful for assaying enzymes in samples too small to be treated by conventional mechanical methods, but gives comparable recoveries of enzyme activities.
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PMID:An enzymatic lysis procedure for the assay of enzymes in Thiobacillus A2. 664 82

Although human milk generally contains higher levels of enzymes than bovine milk, little definitive information is available concerning their role or significance. The enzyme levels in human milk as compared to bovine milk and levels in human colostrum versus normal milk are summarized. The few most widely studied human milk enzymes are discussed in more detail. Evidence is presented to support the views that 1) lipoprotein lipase and ribonuclease are probably spilled into the milk from the blood; 2) lysozyme is spilled from the secretory epithelial cells; 3) lactate and malate dehydrogenases, glucose-6-phosphate dehydrogenase, and lactose synthetase are synthesized in the mammary gland in response to hormonal stimuli; and 4) bile salt stimulated lipase, diastase, protease, and lysozyme are present in sufficient quantities to aid infants in growth and nutrition. Consideration must be given to standardizing the various enzyme assay procedures and activity units so that meaningful comparisons between various studies could be made.
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PMID:Role and significance of enzymes in human milk. 740 88

This study evaluated the effect of sulfuric acid aerosol exposure for 2 consecutive days on seven human biochemical blood parameters. A total of 20 human subjects were exposed to 100 micrograms/m3 (0.033 microM) sulfuric acid aerosol (0.5 microns mean mass diameter) for 4 hr/day for 2 consecutive days. A total of 17 human subjects were exposed to 4 hr of ambient air on both exposure days. The chemical blood parameters were measured pre- and post-exposure, and 20 hr after the second exposure: serum glutathione, red blood cell glutathione reductase, red blood cell glucose-6-phosphate dehydrogenase, lysozyme, serum glutamic oxaloacetic acid transaminase, serum vitamin E, and 2, 3-diphosphoglycerate. The results indicate no significant response in any of the seven biochemical blood parameters measured. At this level, repeated exposure did not over-burden the upper airway defenses against acid aerosol.
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PMID:Biochemical effects of sulfuric acid mist inhalation by human subjects while at rest. 744 96

Therapeutic concentrations (0.3-1.5 mgL-1) of pentamidine isethionate, normally obtainable in-vivo after parenteral administration of the drug, did not affect the in-vitro activity of the enzymes lysozyme, beta-glucuronidase or myeloperoxidase released from zymosan-activated human neutrophilic granulocytes. At concentrations of 0.7, 1.1 and 1.5 mgL-1, activity of cytosolic enzymes lactate dehydrogenase and glucose-6-phosphate dehydrogenase were reduced relative to untreated cells (P < 0.001 and P < 0.01, respectively), but not in a dose-dependent fashion. Cell viability, as determined by dye-exclusion remained unaffected.
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PMID:Selective effects of pentamidine on cytosolic and granule-associated enzyme release from zymosan-activated human neutrophilic granulocytes. 808 18


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