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)

The photodynamic inactivation of lysozyme in air saturated H2O and D2O (phosphate buffer 0.05 M, pH 7.0) in the presence of methylene blue and riboflavin has been studied. When H2O was replaced by D2O a great increase in the rate of photoinactivation of lysozyme was observed. This finding, together with the fact that photooxidation is inhibited by singlet oxygen quenchers like NaN3, suggests that these reactions occur via a singlet oxygen mechanism. During the course of the studies of the riboflavin sensitized photoinactivation of lysozyme, it was found that riboflavin is strongly bound to the enzyme as a result of illumination. This finding would explain the higher quantum yield observed when riboflavin is used, although this dye is bleached during irradiation.
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PMID:Light-induced binding of riboflavin to lysozyme. 59 15

The effect of various polycations on the immune response potentiated with poly I:C was studied. It was found that low molecular weight polycations had no potentiating effect. Polylysine was ineffective whereas protamine was superior to lysozyme, poly-arginine, poly-histidine, DEAE-Dextran and histone. A foot-and-mouth disease trivalent vaccine composed of strains A24 Cruzeiro, O1 Caseros and C2 Resende elicited no immune response in swine when adjuvanted with aluminium hydroxide but was effective when emulsified in oil. In general, the immune response was potentiated ten-fold when the emulsion contained poly I:C. The antibody production was in most cases further potentiated by a factor of ten when the nucleic acid double-strand was complexed with 1 : 10 (w/w) DEAE-Dextran. Protamine was as effective, or perhaps even more, than DEAE-Dextran to this effect. Guinea pigs vaccinated with a water-in-oil emulsion type monovalent C3 vaccine showed an increase in antibody production when the vaccine contained poly I:C or poly I:C complexed with 1 : 10 (w/w) protamine.
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PMID:Potentiation of FMD vaccines with polycationic-nucleic acid complexes. 59 39

The observed rate constants for base-catalyzed hydrogen exchange reactions between solvent water and peptide nitrogen in lysozyme, ribonculease A, oxidized ribonuclease A, and poly(DL-lysine) are all enhanced by an increase in pressure. Activation volumes have been calculated from the pressure effect on these rate constants. For the folded proteins lysozyme and ribonuclease A, deltaV for base-catalyzed exchange changes from about +9 ml/mol at atmospheric pressure -3 ml/mol at 2500 kg/cm2. The same quantity, determined for the random coil polypeptides oxidized ribonuclease A and poly(DL-lysine), does not show this dependence upon pressure. These effects can be understood either in terms of solvent penetration on the folded proteins or the onset of a small degree of pressure induced unfolding. Possible mechanisms by which such penetration could occur are discussed.
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PMID:Pressure effects on folded proteins in solution. Hydrogen exchange at elevated pressures. 63 47

The object of this work was to prepare deuterated growth media and to adapt Micrococcus lysodeikticus to a medium containing deuterated-substituted organic substances and deuterium oxide instead of water. M. lysodeikticus was grown on a medium prepared from the "deuterated-cells" of Chlorella, and was capable of absorbing selectively protons from such a medium containing high concentrations of deuterium. Its deuterated cells ("monsters") produced structures consisting of several (up to 8) smaller cells, angular in shape and having a thicker (2--3 times) cell wall. Apparently, adaptation to a deuterated medium is accompanied with changes in the cell wall biosynthesis as a result of which the separation of daughter cells is interfered with in the course of cell division, and the cells are more resistant to the action of lysozyme.
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PMID:[Growth of Micrococcus lysodeikticus bacteria on a deuterated medium]. 70 45

Liopolysaccharides were prepared from six organisms by the use of two cell-disruption procedures before conventional phenol-water extraction. Disruption of cells by grinding with glass beads or by digestion with hen egg white lysozyme before phenol extraction facilitated rapid purification and greater yields of lipopolysaccharide. Pretreatment of cells with lysozyme in the presence of ethylenediaminetetraacetic acid was the most efficient method in terms of lipopolysaccharide yield and ease of preparation. Increase in lipopolysaccharide yield achieved by use of the lysozyme method, compared with the conventional phenol extraction, varied from 1.7- to 12.4-fold. Preparations were designated as pure according to several criteria and were judged not to have undergone changes as a result of prephenol extraction procedures.
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PMID:Improved techniques for the preparation of bacterial lipopolysaccharides. 81 82

A remarkable resemblance between the appearance of opacity in lysozyme--salt water mixtures and the development of opacity in cold cataract in the young rat lens is strong evidence that cold cataract is fundamentally a phase separation of the "protein-water binary mixture" in the lens.
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PMID:Phase separation of a protein-water mixture in cold cataract in the young rat lens. 88 36

The state of bound water in crystalized lysozyme was studied by four techniques: electret thermal depolarization currents, thermal-stimulated pressure, isothermal polization decay, and thermogravimetry. Hydration levels ranged from 0 to 40 mg water/g protein. Desorption of bound water dipoles was found to be the main process responsible for electrical depolarization. Two different binding sites for water were identified with long relaxation times at room temperature (order 10(2)s) and activation energies of 0.34 plus or minus 0.02 eV and 0.55 plus or minus 0.04 eV.
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PMID:Thermal-stimulated pressure and current studies of bound water in lysozyme. 91 84

Density measurements have been made on aqueous lysozyme solutions at 20, 25, and 30 degrees. The apparent specific volumes, phi v, and expansibilities, phi e, have been determined from the density measurements and fitted to a function of concentration (weight per cent). Sound velocities and heat capacities have also been measured for various concentrations of lysozyme-water solutions at 25 degrees. From the density, expansibility, heat capacity, and sound velocity data at 25 degrees, the isothermal compressibility, phi k, for the lysozyme solutions have been calculated over a range of concentrations. All the physicochemical properties measured were found to be a linear function of the weight per cent of lysozyme. The number of water molecules hydrated to 1 mol of lysozyme was estimated from the volume and compressibility and found to be 162 at 25 degrees.
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PMID:Partial specific volume, expansibility, compressibility, and heat capacity of aqueous lysozyme solutions. 93 18

The hydroxyl groups of poly(ethyleneglycol) have been esterified (partly) with a number of carboxylic acids. When these esters are included in dextranpoly(ethyleneglycol)-water biphasic systems the partitions of proteins and membranes between the two phases (and the interface) are in some cases strongly affected. The affinity of serum albumin for the poly(ethyleneglycol)-rich phase is strongly increased when the fatty acid group consists of more than 10 carbon atoms. The partition also depends on the number of double bonds in the fatty acid. A corresponding relationship is found for membranes from spinach chloroplasts. The partitions of ovalbumin, lysozyme (EC 3.2.1.17) and ribonuclease (EC 3.1.4.22) are not influenced by the fatty acid esters. Esters of dibasic carboxylic acids show a minute but marked effect on the partition of proteins in general while malate and tartrate esters affect strongly the partition of chloroplast membranes. The partitions of both proteins and membranes are influenced by poly(ethyleneglycol) deoxycholate. Experiments with malate dehydrogenase (EC 1.1.1.37), lactate dehydrogenase (EC 1.1.1.27), fumarase (EC 4.2.1.2), enolase (EC 4.2.1.11) and glutamate-ocaloacetate transaminase (EC 2.6.1.1) show that their partitions, measured on enzymic activity basis, is changed when esters of benzoic, linolenic, tartaric or deoxycholic acid are included in the biphasic system. The mechanism behind the effect of the esterified poly (ethyleneglycol) on the partition of biomaterial, in this type of aqueous biphasic systems, is discussed in terms of a direct binding of the esters to the partitioned material.
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PMID:The effect of poly(ethyleneglycol) esters on the partition of proteins and fragmented membranes in aqueous biphasic systems. 99 68

Treatment of human enamel powder with cyclic trimetaphosphate or linear tripolyphosphate changes subsequent adsorption of amylase, lysozyme, and salivary protein from aqueous solutions. Treated enamel samples adsorb more lysozyme, less amylase, and more salivary protein (at concentrations exceeding 12 mug/ml) than controls treated with distilled water.
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PMID:Comparison of the effects of linear and cyclic phosphates on the adsorption of proteins by human enamel. 105 53


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