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)

Analyses of whole and parotid saliva were performed in ten patients with subjective symptoms resembling galvanic pain and in their eight asymptomatic counterparts. Salivary flow rates, protein, IgA, lysozyme, sodium, potassium, chloride, calcium phosphate, copper, and magnesium contents were measured. The concentrations of protein, sodium, chloride, and phosphate in the whole saliva of the patients with symptoms were significantly higher, but concentrations of calcium, magnesium, and IgA were lower than in the asymptomatic controls. In parotid saliva, too, protein, lysozyme, and calcium concentrations were significantly altered in patients with oral symptoms. The analysis of free amino acids serine, proline, glutamic acid + glutamine, and glycine in the whole saliva did not show any significant differences between the two groups studied. The results suggest the importance of salivary contents in the development of oral soreness. Such changes in the salivary constituents could modulate the amount and character of the salivary macromolecules absorbed onto the teeth. This could lead to passivation or activation of the surfaces in metallic restorations and consequently to the onset of the intraoral electric currents.
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PMID:Salivary content of patients with subjective symptoms resembling galvanic pain. 659 63

We have compared the oxidative renaturation of reduced hen egg white lysozyme promoted by Cu(II) + O2 with that promoted by a glutathione redox buffer. The progress curves for protein fluorescence, circular dicroism, thiol oxidation, hydrodynamic volume, and enzymic activity were determined for both regeneration systems. All of these processes were more rapid in the glutathione regeneration than in the copper-catalyzed. Comparison of the two systems was carried out by normalizing the progress curves with a coordinate system where "time" is replaced by "extent of protein thiol oxidation." While similar progress curves were obtained for circular dichroism, the two systems produced distinctly different progress curves for enzymic activity, fluorescence, and gel permeation chromatographic reflection of protein hydrodynamic volume. We infer that all these differences result from differences in relative amounts and/or kind of reaction intermediates. Thus, there are substantial differences between the renaturation mechanisms of the glutathione- and the copper-promoted systems.
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PMID:Multiple parameter kinetic studies of the oxidative folding of reduced lysozyme. 661 47

Groups of rabbits were exposed to chlorides of nickel, cadmium, copper, and cobalt at concentrations ranging from 0.2 to 0.6 mg/m3 (as metal) for 4-6 weeks (5 days/week, 6 hr/day). Activity of lysozyme (muramidase) in lavage fluid, in alveolar macrophages, and in culture medium from macrophages incubated at 37 degrees C for 1 and 20 hr was estimated using the lyso-plate technique, agar plates with heat-killed Micrococcus lysodeikticus. In the nickel-exposed rabbits lysozyme activity in the mucous membrane from the left main bronchus was also estimated. Following nickel exposure the lysozyme level was significantly decreased in lavage fluid, macrophages, and in culture medium from incubated macrophages but remained unchanged in the mucous membrane. After exposure to cadmium, copper, and cobalt, lysozyme levels increased or were unchanged.
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PMID:Lysozyme levels in rabbit lung after inhalation of nickel, cadmium, cobalt, and copper chlorides. 674 35

Employing equilibrium dialysis, the binding ability of nickel, copper, and chromium from the corrosion of Biobond, Sybraloy, and Vitallium dental alloys in an inorganic saliva to glycoprotein, mucin, amylase, and lysozyme is reported. Binding was highest with copper to glycoprotein at 5.0 M Cu/M protein, followed by nickel at 1.2 M Ni/M protein, and by chromium at 0 M Cr/M protein. Tin products did not succumb to dialysis. The binding to all types of proteins exhibited molar ratios of about equal magnitudes except in lysozyme where binding was very low, most likely due to its high isoelectric point. Protein--protein interactions for amylase were higher, which hindered the nickel binding at lower protein concentrations. Peaks in glycoprotein binding vs pH behaviour occurred for copper at pH = 6 and for nickel at pH = 7. For glycoprotein and mucin, binding is taken to occur via the sialic acid carboxylate groups and for amylase via the imidazole groups of the histidine residues. It is thought that in order for copper to bind with the same number of sites as does occur with nickel, ligands of the form CuCl-CuCl2 are generated. The size of hexahydrate ligands of chromium are large which may not permit attachment onto binding sites.
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PMID:The binding of corroded metallic ions to salivary-type proteins. 686 Jul 59

We have used the electron paramagnetic resonance of Cu2+ bound in a tetragonal single crystal of hen egg-white lysozyme to obtain the electron nuclear double resonance spectra of protons in the vicinity of the Cu2+ at the site designated as B by Teichberg et al. [Teichberg, V. I., Sharon, N., Moult, J., Smilansky, A. & Yonath, A. (1974) J. Mol. Biol. 87, 357-368]. The values of the hyperfine interaction parameters and the coordinates of eight protons are reported. The configuration of the H2O molecules coordinated to the Cu2+ and their relationships to the protein molecule structure are discussed.
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PMID:Electron nuclear double resonance spectroscopy of a hen egg-white lysozyme--Cu2+ complex in tetragonal single crystals. 694 64

The main pathological feature of experimental legionellosis produced by the intraperitoneal inoculation of guinea-pigs was a fibrinopurulent peritonitis, especially over the liver and spleen. Foci of necrosis were present in these organs from the second to seventh day after infection. Early biochemical changes in the serum included significant decreases in the concentration of zinc and iron, and increases in copper and triglycerides. Phenylalanine to tyrosine ratios increased strikingly, but free amino acid decreased slightly. The total protein concentration did not change, but acute-phase proteins increased. Serum lysozyme activity increased as leucocytosis developed but fell during the subsequent leucopenia. In the later stages of the disease the activity of alkaline phosphatase, gamma-glutamyl transpeptidase, and creatine kinase decreased; that of dehydrogenases and transaminase increased.
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PMID:Pathological and biochemical features of Legionella pneumophila infection in guinea-pigs. 712 Mar 55

The authors investigated SigA, Lysozyme (muramidase), albumin and copper levels in the saliva of sixteen children in the course of the day. A total of nine blood samples was taken in three-hour intervals from each child. Statistically highly significant changes were found in SIgA with a minimal average at 11 a.m. and maximum at 5 a.m. In albumin the maximum was recorded already at 11 p.m., while the minumum was at 11 a.m. The changes of copper values were different, with the maximum at 11 a.m. and minimum at 2 a.m., with smallest individual differences of mean daily levels. Lysozyme displayed an individual variability of levels and the lowest correlation with the investigated rhythms. A statistically significant difference was found only between samples collected during day- and night time. The findings are discussed from the aspects of other relations which might influence the assessed values.
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PMID:Circadian changes of the SIgA, lysozyme, albumin and copper content of saliva. 722 23

The interaction between hen egg-white lysozyme and Cu(II) or Co(II) cations has been studied by dilatometry, equilibrium dialysis-differential refractometry and viscometry at different metal cation concentrations. Delta V isotherms in copper and cobalt solutions have been obtained from dilatometry. Preferential adsorption parameters and specific viscosity have been determined from refractometric and viscosimetric measurements. It has been observed that this interaction produces structural alterations in lysozyme. The magnitude of these conformational changes depends on the metal ion and protein concentration. The results obtained using the three techniques are in good agreement.
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PMID:Dilatometric, refractometric and viscometric study of lysozyme-cation interaction. 732 52

The mechanism of irreversible inactivation of lysozyme at neutral pH at 100 degrees C, and effects of additives on the inactivation were investigated. The thermoinactivation of lysozyme at neutral pH was caused by intra- and intermolecular disulfide exchange and the production of irreversibly denatured lysozyme, which was destabilized by multiple chemical reactions other than disulfide exchange. In addition, independently, deamidation slightly affected the inactivation by causing a decrease of electrostatic interaction between positive charges of lysozyme and negative charges of the bacterial cell wall. As for the effects of additives on the inactivation, a small amount of copper ion suppressed intra- and intermolecular disulfide exchange by catalyzing air oxidation of heat-induced trace amounts of free thiols, and organic reagents (acetamide, ethanol, and glycerol) changed the mechanism of the inactivation to that under acidic conditions by shifting the pKa values of dissociable residues and also suppressed intermolecular disulfide exchange by decreasing hydrophobic interactions.
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PMID:Effects of additives on irreversible inactivation of lysozyme at neutral pH and 100 degrees C. 760 27

Riboflavin is known to generate superoxide anion upon photoillumination and in the presence of Cu(II) causes fragmentation of DNA. In the present study we examined the effect of riboflavin and Cu(II) on bovine serum albumin, invertase and lysozyme. Using fluorescence quenching experiments, it is shown that riboflavin binds to protein and causes fragmentation which in the presence of Cu(II) is enhanced. Using neocuproine as the Cu(I) sequestering reagent, it has also been shown that Cu(I) is an essential intermediate in the protein fragmentation reaction. Results obtained with various scavengers of active oxygen species strongly suggest that the species predominantly responsible for protein breakage is hydroxyl radical.
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PMID:Enhanced protein degradation by photoilluminated riboflavin in the presence of Cu(II). 770 5


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