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

1. The effects of AL0671, a novel potassium channel opener, on protein glycation and low-density lipoprotein (LDL) oxidation were tested. 2. AL0671 dose-dependently inhibited both fluorescence development of bovine serum albumin and cross-linking of lysozyme. These inhibitory effects for glycation were no less potent than aminoguanidine. 3. AL0671 dose-dependently inhibited both increase in negative charge and apo B-100 fragmentation during incubation of LDL with Cu2+. In addition, AL0671 significantly decreased the LDL degradation in rat peritoneal macrophages. 4. Neither pinacidil nor levcromakalim inhibited protein glycation and LDL oxidation. 5. Antioxidant properties of AL0671 might be due to its potent electron-donating ability, and this agent is expected to be useful for hypertensive diabetes.
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PMID:AL0671, a new potassium channel opener, inhibits nonenzymatic glycation of protein and LDL oxidation. 891 39

Two extracellular chitinases (FI and FII) were purified from the culture supernatant of Pseudomonas aeruginosa K-187. The molecular weights of FI and FII were 30,000 and 32,000, respectively, by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and 60,000 and 30,000, respectively, by gel filtration. The pIs for FI and FII were 5.2 and 4.8, respectively. The optimum pH, optimum temperature, pH stability, and thermal stability of FI were pH 8, 50 degrees C, pH 6 to 9, and 50 degrees C; those of FII were pH 7, 40 degrees C, pH 5 to 10, and 60 degrees C. The activities of both enzymes were activated by Cu2+; strongly inhibited by Mn2+, Mg2+, and Zn2+; and completely inhibited by glutathione, dithiothreitol, and 2-mercaptoethanol. Both chitinases showed lysozyme activity. The purified enzymes had antibacterial and cell lysis activities with many kinds of bacteria. This is the first report of a bifunctional chitinase/lysozyme from a prokaryote.
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PMID:Purification and characterization of two bifunctional chitinases/lysozymes extracellularly produced by Pseudomonas aeruginosa K-187 in a shrimp and crab shell powder medium. 902 18

In these investigations, the influence of a range of experimental parameters on the isothermal characteristics of hen egg white lysozyme (HEWL) and human serum albumin (HSA) adsorbed to several different adsorbents has been examined. The adsorbents were selected to encompass the same basic types of silica support matrices, but with the ligand properties and surface characteristics adjusted so that the dominant mode of interaction between the protein and the ligand involved either electrostatic binding (i.e. as ion-exchange interaction with polyaspartic acid immobilised onto glycidoxypropyl-modified Fractosil 1000), mixed-mode binding with both hydrophobic and electrostatic effect contributing to the protein-ligand interaction (i.e. as dye-affinity interactions with Cibacron Blue F3G-A immobilised onto Lichroprep DIOL or onto glycidoxypropyl-modified Fractosil 1000), or lone pair coordination binding (i.e. as immobilised metal ion affinity (IMAC) interactions with Cu2+ ions complexed with iminodiacetic acid immobilised onto glycidoxypropyl-modified Fractosil 1000). In each case, the adsorbents exhibited similar ligand densities and had the same particle size ranges and silica surface pretreatment. The effect of the ionic strength of the adsorption buffer and temperature on the isothermal adsorption behaviour under batch equilibrium binding conditions of the two test proteins were determined. Consistent with previous observations with soft gel ion exchangers and triazine dye-based adsorbents that are used in packed bed chromatographic systems, the capacities of the silica-based ion-exchange adsorbents, as well as the Cibacron Blue F3G-A dye affinity adsorbents, for both HSA and HEWL were reduced as the salt concentration was increased under batch equilibrium binding conditions. Moreover, with both of these classes of adsorbents, as the ionic strength was increased under constant temperature conditions, the isothermal adsorption dependencies progressively approximated more closely a Langmuirean model of independent binding site interactions, typical of a mono-layer binding process. In contrast, with the silica-based immobilised metal ion affinity adsorbents as the ionic strength was increased the adsorption behaviour appeared to follow a Freundlich model, indicative of positive cooperativity in the binding process. In parallel experiments, the effect of changes in temperature under iso-ionic strength conditions was examined. With increasing temperature, different patterns of isothermal adsorption behaviour for both test proteins were observed, with the magnitude of these trends depending on the type of interaction involved between the immobilised ligand and the protein. Utilising first order Van't Hoff relationships to analyse the experimental data for these protein-ligand interactions, the apparent changes in enthalpy and entropy for these interactions have been derived from the dependency of the change in the apparent Gibbs free energy on 1/T.
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PMID:Comparative studies on the isothermal characteristics of proteins adsorbed under batch equilibrium conditions to ion-exchange, immobilised metal ion affinity and dye affinity matrices with different ionic strength and temperature conditions. 912 17

The use of high capacity micron-sized non-porous magnetic metal chelator adsorbents for the direct recovery of a recombinant metal-binding protein from crude liquors is described. Selectivity and interaction strength of magnetic chelator particles were assessed using a set of native proteins with known behaviour towards commercially available immobilised metal chelate adsorbents. Particles charged with Cu2+ were highly effective in recovering a recombinant histidine-tailed T4 lysozyme fusion protein directly from crude E. coli extracts in a single step. Levels of recovery and purity were high and compared favourably with those achieved by chromatography of pre-clarified extracts on Cu(2+)-IDA Sepharose. The magnetic approach offers advantages such as the avoidance of clarification to prevent fouling of chromatography columns, steps that become especially significant at large scale. By detailed characterisation of the magnetic chelators the practical use of tailed T4 lysozyme for repeated production of periplasmic products is a realistic prospect.
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PMID:Characterisation of non-porous magnetic chelator supports and their use to recover polyhistidine-tailed T4 lysozyme from a crude E. coli extract. 918

In this investigation, employing a highly sensitive microcalorimeter, we measure the influence of pH value and salt concentration on the heat of interaction between lysozyme and CS-IDA-Cu(II) gel. The direct enthalpy measurement of the interaction provides thermodynamic information regarding the binding behavior of lysozyme toward the immobilized metal ion. The binding enthalpy altered by adsorbed lysozyme at various pH values and salt concentrations are measured. The findings, along with the reported binding isotherm, are discussed herein.
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PMID:Microcalorimetric Studies of the Interactions of Lysozyme with Immobilized Cu(II): Effects of pH Value and Salt Concentration 924 Nov 40

The chromatographic selectivity of the immobilized chelate system, 1,4,7-triazocyclononane (tacn), complexed with the borderline metal ions Cu2+, Cr3+, Mn2+, Co2+, Zn2+, and Ni2+ has been investigated with hen egg white lysozyme, horse heart cytochrome c, and horse skeletal muscle myoglobin, as well as proteins present in partially fractionated preparations of human plasma. The effects of ionic strength and pH of the loading and elution buffers on protein selectivities of these new immobilized metal ion affinity chromatographic (IMAC) systems have been examined. The results confirm that immobilized Mn;pl-tacn sorbents exhibit a novel type of IMAC behavior with proteins. In particular, the chromatographic properties of these immobilized M(n+)-tacn ligand systems were significantly different compared to the IMAC behavior observed with other types of immobilized tri- and tetradentate chelating ligands, such as iminodiacetic acid, O-phosphoserine, or nitrilotriacetic acid, when complexed with borderline metal ions. The experimental results have consequently been evaluated in terms of the additional contributions to the interactive processes mediated by effects other than solely the conventional lone pair Lewis soft acid-Lewis soft base coordination interactions, typically found for the IMAC of proteins with borderline and soft metal ions, such as Cu2+ or Ni2+.
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PMID:Protein selectivity with immobilized metal ion-tacn sorbents: chromatographic studies with human serum proteins and several other globular proteins. 944 41

Hypochlorite-oxidized low-density lipoprotein ((-)OCl-LDL) has been shown to stimulate various functions of human polymorphonuclear leukocytes (PMNLs). Incubation of PMNLs with (-)OCl-LDL (produced by incubation of 0.4 mM LDL cholesterol with 1 mM NaOCl for 40 min at 37 degrees C) but not native or copper-oxidized LDL induced a substantial generation of reactive oxygen species (ROS) as measured by means of chemiluminescence with one peak at 10-12 min. Upon stimulation with (-)OCl-LDL about 70% of ROS (hydrogen peroxide and superoxide anion) were released from the cells into the extracellular environment. The (-)OCl-LDL-induced increase of the respiratory burst was dependent upon the dose, exposure time, and extent of LDL oxidation. Cytochalasin B, an inhibitor of phagocytosis, markedly diminished the LDL-induced ROS generation to nearly 40% of control values. (-)OCl-LDL enhanced the adhesion of PMNLs to human umbilical venous endothelial cells 2.5-fold as compared to native LDL and promoted the secretion of the active granule enzymes lysozyme and beta-glucuronidase. Together, the results suggest a potential role of LDL-activated PMNLs in initiating and/or maintaining the inflammatory process during the early phase of atherosclerotic lesion development. Alternatively, PMNLs may also play a protective role by phagocytosing oxidized LDL and, thus, preventing further detrimental atherogenic effects of oxidized LDL.
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PMID:Hypochlorite-modified low-density lipoprotein stimulates human polymorphonuclear leukocytes for enhanced production of reactive oxygen metabolites, enzyme secretion, and adhesion to endothelial cells. 954 3

The formation of three-dimensional structures of double-stranded nucleic acid and polynucleotide molecules, fixed in the structure of liquid-crystalline dispersions and bridged by polymeric chelate complexes is described. The bridging elements consist of alternating daunomycin molecules and copper ions. It is shown that these bridges between nucleic acid molecules stabilize cholesteric structures of the DNA liquid-crystalline dispersion. The formation of polymeric chelate bridges is accompanied by a remarkable increase of the intense circular dichroism (CD) band characteristic of the DNA-daunomycin cholesterics. These bridges are destabilized by a number of biologically relevant compounds and macromolecules, such as ascorbic acid, homocarnosine, bovine serum albumin and lysozyme. The dramatic change in the optical activity of the liquid-crystalline dispersions upon addition of these compounds makes them easily detectable. The sensitivity of the method, in the range of analytic concentration 10(-4)-10(-8) M, depends on the nature of the compound being tested. The response of bridged DNA structures to biological effectors observed here foresees their further development as biosensor devices for detecting the presence of biologically and pharmacologically relevant compounds.
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PMID:Sensing biological effectors through the response of bridged nucleic acids and polynucleotides fixed in liquid-crystalline dispersions. 964 66

This study extends previous research on the interaction of biomaterials with immobilized Cu(II) by isothermal titration calorimetry (ITC) on Fe(III). The difference of the binding behavior of protein with that of the immobilized metal ions is also discussed. For the immobilized Fe(III), ITC results show that the adsorption enthalpy at a constant pH value decreased as the NaCl concentration increased and also decreased with the pH values at constant NaCl concentrations. The adsorption enthalpy become negative under higher pH values or higher salt concentrations indicating the adsorption process is partly driven by the enthalpy. The enthalpy of lysozyme with Fe(III) is higher than that with Cu(II) implying that the heat required for the dehydration of Cu(II) is lower than for the dehydration of Fe(III) and/or that the heat generated from the formation of the coordination with Cu(II) is higher than with Fe(III). In addition, the comparison of different immobilized metal ions corresponding to the equilibrium binding affinity suggests that the binding force of lysozyme with Cu(II) is higher than with Fe(III). This study presents the chemical differences between the binding affinity and the adsorption enthalpy of lysozyme interacting with the immobilized metal ions. The binding and thermodynamic data presented in this study elucidate the mechanism and process of lysozyme binding with immobilized metal ions. In addition, the thermodynamic characteristic functions provide valuable information enabling a more thorough understanding of protein adsorption at the immobilized metal ion affinity surface. Copyright 1999 Academic Press.
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PMID:Microcalorimetric Studies of the Interactions of Lysozyme with Immobilized Metal Ions: Effects of Ion, pH Value, and Salt Concentration. 1033 77

The cDNA, coding for the first metal-binding domain (MBD1) of Menkes protein, was cloned into the T7-system based vector, pCA. The T7 lysozyme-encoding plasmid, pLysS, is shown to be crucial for expression, suggesting that the protein is toxic to the cells. Adding copper to the growth medium did not affect the plasmid stability. MBD1 is purified in two steps with a typical yield of 12 mg.L-1. Menkes protein, a P-type ATPase, contains a sequence GMXCXSC that is repeated six times, at the N-terminus. The paired cysteine residues are involved in metal binding. MBD1 has only two cysteine residues, which can exist as free thiol groups (reduced), as a disulphide bond (oxidized) or bound to a metal ion [e.g. Cu(I)-MBD1]. These three MBD1 forms have been investigated using CD. No major spectral change was seen between the different MBD1 forms, indicating that the folding is not changed upon metal binding. A copper-bound MBD1 was also studied by EPR, and the lack of an EPR signal suggests that the oxidation state of copper bound to MBD1 is Cu(I). Cu(I) binding studies were performed by equilibrium dialysis and revealed a stoichiometry of 1 : 1 and an apparent Kd = 46 microM. Oxidized MBD1, however, is not able to bind copper. Different copper complexes were investigated for their ability to reconstitute apo-MBD1. Given the same total copper concentration CuCl43- was superior to Cu(I)-thiourea (structural analogue of metallothionein) and Cu(I)-glutathione (used at fivefold higher copper concentration) although the latter two were able to partially reconstitute apo-MBD1. Cu(II) was not able to reconstitute apo-MBD1, presumably due to Cu(II)-induced oxidation of the thiol groups. Based on our results, glutathione and/or metallothionein are likely candidates for the in vivo incorporation of copper to Menkes protein.
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PMID:Expression, purification and copper-binding studies of the first metal-binding domain of Menkes protein. 1049 Nov 37


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