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

---

Query: EC:3.2.1.17 (lysozyme)
21,489 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Effects of 10-30% (v/v) of dimethyl sulfoxide, glycerol, and ethylene glycol on the H-O-H bending vibration of water and the amide I bands of horse heart cytochrome c and chicken egg white lysozyme in 25 mM sodium phosphate buffer (pH 7.4) were examined at 20 degrees C by Fourier transform infrared spectroscopy. The H-O-H bending mode of water was strongly affected by these cryoprotectant solvents. Increasing the concentration of cryosolvents from 0 to 30% shifts the water bending band maximum from 1645 to about 1650 cm-1. Second-derivative analysis reveals significant changes in conformation-sensitive amide I regions of lysozyme ascribed to alpha-helix (1657 cm-1), turn (1674 cm-1), and unordered (1646 cm-1) structures; each cryosolvent increases the intensity of the 1657 cm-1 band at the expense of bands at 1674 and 1646 cm-1. No changes in spectra deemed significant were observed for cytochrome c under the same conditions. There is no spectral evidence of structural randomization of proteins due to the presence of these cryosolvents. Cryosolvent-induced changes in secondary structure of proteins may result from changes in water structure which, in turn, perturb the structure of the protein and/or from direct interactions between cryosolvent and protein.
...
PMID:Effects of dimethyl sulfoxide, glycerol, and ethylene glycol on secondary structures of cytochrome c and lysozyme as observed by infrared spectroscopy. 762 25

The effect of ionic strength and ethylene glycol on the adsorption of bovine serum albumin (BSA) or lysozyme by a commercial aluminium hydroxide or aluminium phosphate adjuvant was studied at pH 7.4 and 25 degrees C. The adsorption of BSA by aluminium hydroxide adjuvant and lysozyme by aluminium phosphate adjuvant was found to be inversely related to ionic strength. This indicates that electrostatic attractive forces contribute to adsorption. The adsorption of lysozyme by aluminium phosphate adjuvant was reduced by the addition of ethylene glycol. However, no change in the adsorption of BSA by aluminium hydroxide adjuvant was noted when up to 40% ethylene glycol was present. This behaviour indicates that hydrophobic forces contribute to the adsorption of lysozyme but not of BSA. However, virtually no adsorption was observed when the protein and the adjuvant had the same surface charge. Thus, attractive forces may not be sufficient to produce adsorption of an antigen by an aluminium-containing adjuvant if electrostatic repulsive forces are present.
...
PMID:Contribution of electrostatic and hydrophobic interactions to the adsorption of proteins by aluminium-containing adjuvants. 776 76

Human lysozyme dimers were prepared by the intermolecular cross-linking of the monomer that contained the mutation of either Arg41 to Cys or Ala73 to Cys with a divalent maleimide compound. Among the three kinds of possible dimers only R41C-R41C dimer, in which the two catalytic clefts can come close to each other due to the proximity of the conjugation site to the active sites, turned out to be 2.3 times more specific to a polymer substrate, ethylene glycol chitin, as compared to an oligomer substrate, PNP-(GlcNAc)5. The result indicates that it is possible to alter the substrate specificity of an enzyme by artificially controlling the orientation of the active sites.
...
PMID:Alteration of the substrate specificity of human lysozyme by site-specific intermolecular cross-linking. 798 87

Surface tension measurements were carried out at 20 degrees C by a capillary drop-weight method on aqueous solutions of sodium glutamate (NaGlu), lysine hydrochloride (LysHCl), potassium aspartate (KAsp), arginine hydrochloride (ArgHCl), lysylglutamate (LysGlu), argininylglutamate (ArgGlu), guanidinium sulfate, trehalose, trimethylamine N-oxide (TMAO), dimethyl sulfoxide, 2-methyl-2,4-pentanediol (hexylene glycol), and poly(ethylene glycol)s of molecular weights 200, 400, 600, and 1000. All of the salts and the sugar increased the surface tension of water, while the last four compounds decreased it, with 2-methyl-2,4-pentanediol lowering it most effectively and TMAO being the least effective. The preferential hydration of bovine serum albumin (BSA) and lysozyme was measured in KAsp, ArgHCl, LysGlu, and ArgGlu. The high values of preferential hydration found in all cases, except for BSA in ArgHCl, suggest that they should stabilize protein structure, as had been found for lysine hydrochloride and monosodium glutamate [Arakawa, T., & Timasheff, S. N. (1984) J. Biol. Chem. 259, 4979-4986]. A correlation was found for both BSA and lysozyme in KAsp, NaGlu, LysHCl, ArgGlu, and LysGlu between the surface tension effect and the observed preferential interactions, indicating that the change in the surface free energy of the protein-containing cavity due to the surface tension increase for water by these amino acid salts contributes dominantly to the observed increase in the chemical potential of the protein by their addition. The lack of a correlation observed for BSA, but not lysozyme, in ArgHCl at low concentrations where preferential binding is close to zero suggests, however, that the surface tension effect is not the sole factor involved in the protein-solvent interactions in these amino acid salts. Binding of ArgHCl to BSA, probably through hydrogen bonds between the Arg guanidinium group and peptide bonds, was proposed to occur, the affinity of Arg+ being reduced by electrostatic repulsion when proteins carry a net positive charge, such as is the case with lysozyme. Since the four organic solvent additives also lead to protein preferential hydration, no correlation exists between their preferential interactions and the surface free energy perturbation. Therefore, in their case, the preferential hydration must be ascribed to other factors that overcome the preferential binding expected from the Gibbs adsorption isotherm. The surface tension results, however, are consistent with the binding of the organic solvents to proteins through hydrophobic interactions, explaining, at least in part, the observed concentration dependence of the interactions.
...
PMID:Contribution of the surface free energy perturbation to protein-solvent interactions. 799 78

Genetic transfer mediated by spheroplast formation and fusion in Escherichia coli was studied. Recombination did not occur from spheroplasts prepared by the combined glycine and lysozyme-EDTA treatment described by Coetzee et al. (1979). In contrast, when bacteria were exposed to a sub-inhibitory concentration of polymyxin B (0.5 microgram/ml) during the spheroplast generation phase, recombinants arose at frequencies of 1 x 10(-8) to 2.6 x 10(-8). The incidence of genetic transfer was further increased by adding 0.01 M CaCl2 to the polyethylene glycol fusion mixture (from 9 x 10(-7) to 9 x 10(-8). Finally, when the effects of both polymyxin B and calcium chloride were combined recombinants arose at frequencies of 3.4 x 10(-6) to 7.3 x 10(-7). These findings suggest that the detergent-like action of polymyxin B in removing a large part of the outer membrane enhances plasma membrane availability where fusion can take place.
...
PMID:Genetic recombination by spheroplast fusion in Escherichia coli K12. 829 82

The use of high water content (> 96%) hydrogels obtained from copolymerisation of bovine serum albumin and poly(ethylene glycol) as a controlled release system has been investigated. Such hydrogels allowed release of soluble and hydrophobic substances, even proteins. Release is shown to occur by a diffusion controlled mechanism, leading to half-life times of release ranging between 0.8 hour for theophylline and 4.2 hours for lysozyme, when a 2.4 mm thick disc of BSA-PEG (MW of 10000) was used. The effect of the porosity of the hydrogel on the diffusive properties of theophylline and hydrocortisone has been evaluated by varying the molecular weight of the poly(ethylene glycol). It was shown that poly(ethylene glycol) of high molecular weight leads to more porous hydrogels in which the diffusion is faster.
...
PMID:Drug release from new bioartificial hydrogel. 852 54

The results of the interspecific protoplast fusion between B. thuringensis sub. kurstaki Bt-3701 which has pesticide ability, and B. megaterium var. phosphaticum Bm-107 which has decomposing phosphate activity, were reported. High frequency of protoplast formation and regeneration was obtained with 4h activated Bm-107 treated by 100 micrograms/ml lysozyme, and with 2h activated Bt-3701 treated by 3% glycin and mild temperature. Using 40% PEG and 5% nascent Ca2+ to treat the parential protoplast mixture for 3 min at 37 degrees C, 4 stable fusants were obtained. Biological tests show that they have both pesticide ability and decomposing phosphate activity, but which are weaker than that of parential strains.
...
PMID:[Interspecific protoplast fusion between Bacillus thuringensis Bt-3701 and Bacillus megaterium Bm-107]. 870 82

The effect of nine organic solvents and urea on hen-eggwhite lysozyme-rabbit antilysozyme precipitin reaction was studied at a ratio of the antigen to the antibody of 1:26 by weight in 70 mM sodium phosphate buffer, pH 7.0. The organic solvents used were dioxane, acetonitrile, dimethylsulfoxide, N,N-dimethylformamide, 1-propanol, propylene glycol, trifluoroethanol, ethylene glycol and glycerol. These solvents invariably caused reduction in the amount of protein precipitated during the antigen-antibody reaction. The concentration of an organic solvent, CM, required for 50% reduction in the precipitin reaction value was determined for each organic solvent. Among the nine organic solvents, dioxane was the most potent inhibitor of the precipitin reaction. The nine organic solvents did not cause irreversible inactivation of the antigen and the antibody, and at concentrations used in this study most of them would be nondenaturing. These solvents seem to destabilize the antigen-antibody complex.
...
PMID:Effect of organic solvents on lysozyme-antilysozyme precipitin reaction. 876 Jun 6

Aqueous two-phase systems composed of ethylene oxide/propylene oxide random co-polymers, EO30/PO70 or Ucon (EO50/PO50), in the top phase and dextran T500 in the bottom phase, have been studied. The cloud point diagram for EO30/PO70 in water solution was determined. EO30/PO70 has a cloud point of 32 degrees C at a concentration of 10% (w/w). The phase diagram for the system EO30/PO70-dextran T500-water was determined. Salt effects have been studied on the partitioning of two model proteins, bovine serum albumin and hen egg white lysozyme, in EO30/PO70-dextran and Ucon-dextran systems. Ions with different hydrophobicity, i.e., with different position in the Hofmeister or lyotropic series, were investigated with reference to their effect on protein partition. The counterion hydrophobicity was shown to have a strong influence on the partitioning of BSA and lysozyme. Most extreme partitioning was obtained with hydrophobic (chaotropic) ions like CIO4- and I-. A comparison of protein partitioning between PEG-dextran and EO30/PO70-dextran has been done. A more extreme protein partitioning was obtained in the EO30/PO70-dextran containing system. Temperature-induced phase separation was studied with EO30/PO70 at 45 degrees C. Both BSA and lysozyme were completely partitioned to the water phase formed above the cloud point of EO30/PO70. Model calculations, based on Flory-Huggins theory of polymer solutions, have been done which could reproduce the salt effect on the protein partitioning in aqueous-two phase system.
...
PMID:Effects of ions on partitioning of serum albumin and lysozyme in aqueous two-phase systems containing ethylene oxide/propylene oxide co-polymers. 876 33

The effect of proline on the prevention of trichloroacetic acid (TCA)-induced protein precipitation is studied. It is found that proline at high concentrations (> 4.0 M) completely prevents TCA-induced precipitation of hen egg white lysozyme. Other osmolytes such as ethylene glycol, glycerol and sucrose fail to prevent the TCA-induced precipitation of lysozyme. Viscosity and 1-anilino-8-naphthalene sulphonic acid binding experiments suggest that proline at high concentration forms an ordered supramolecular assembly. Proline is shown to increase the solubility of protein due to formation of such higher order assemblies. A model of the supra-molecular assembly of proline is proposed and a possible in vivo role of the increased levels of proline under water stress is discussed.
...
PMID:Proline is a protein solubilizing solute. 906 63


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>

---