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

Bladen, Howard A. (National Institute of Dental Research, Bethesda, Md.), and Stephan E. Mergenhagen. Ultrastructure of Veillonella and morphological correlation of an outer membrane with particles associated with endotoxic activity. J. Bacteriol. 88:1482-1492. 1964.-Normal, phenol-water extracted, and lysozyme-treated Veillonella cells were embedded in Vestopal W, sectioned, and examined by electron microscopy. Normal cells as well as the phenol-water extract (endotoxin) were examined by negative and positive contrast techniques. In thin sections of normal cells, three separate structural entities were observed surrounding the protoplasm, and were referred to as the outer membrane, the solid membrane, and the plasma membrane. The outer membrane was a membrane composed of two dense layers (30 A) separated by a less-dense layer (20 A), and followed a convoluted and continuous path around the cell. The solid membrane appeared as a taut, dense structure 100 to 500 A wide, and was separated from the outer membrane by up to several hundred Angstroms. The plasma membrane was a unit-type membrane. After cells were treated with phenol-water, the outer membrane was absent, but the cells remained intact owing to the solid membrane. Observation of the phenol-water extract (endotoxin) revealed predominantly circular particles or discs which had approximately the same dimensions in height as the outer membrane had in width. Negatively stained whole cells showed similar structures on their surface. Lysozyme treatment of the cells did not affect the outer membrane; however, the solid membrane became diffuse and often disappeared, suggesting that the outer membrane and the solid membrane were separate structures.
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PMID:ULTRASTRUCTURE OF VEILLONELLA AND MORPHOLOGICAL CORRELATION OF AN OUTER MEMBRANE WITH PARTICLES ASSOCIATED WITH ENDOTOXIC ACTIVITY. 1423 9

OBJECTIVE:To evaluate the effect of drug on chemical degradation of lipopolysaccharide (LPS) from oral anaerobes.METHODS:LPSs from porphyromonas gingivalis (Pg),bacteroides fragilis (Bf) and fusobacteria nucleatum (Fn) were extracted by the hot phenol-water method and purified by the phenol-chloroform-petroleum ether procedure.1.0 ml (200microg) various LPSs were incubated with 2.0 ml various drugs at 37degrees centigrade for 15 or 30 minutes in vitro,respectively.The chemical degradation of LPS was quantitated by limulus synthetic chromogenic substrated method after dialysis.RESULTS:The order of degradation was 30% hydrogen peroxide (H),50% citric acid (C),garlic guice (G),1:1 diluted G,25% C and 3% H,and their efffcts were dose dependent and were time dependent except H but the effect of lysozyme was minimal.CONCLUSION:The study may imply that the dose and the mechanism of various drugs on LPS degradation are different and remains to be elucidated.
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PMID:[The chemical degradation of lipopolysaccharides from oral anaerobes] 1504 37

A major Bacillus anthracis spore coat protein of 13.4 kDa, designated Cot alpha, was found only in the Bacillus cereus group. A stable ca. 30-kDa dimer of this protein was also present in spore coat extracts. Cot alpha, which is encoded by a monocistronic gene, was first detected late in sporulation, consistent with a sigma(K)-regulated gene. On the basis of immunogold labeling, the protein is in the outer spore coat and absent from the exosporium. In addition, disruption of the gene encoding Cot alpha resulted in spores lacking a dark-staining outer spore coat in thin-section electron micrographs. The mutant spores were stable upon heating or storage, germinated at the same rate as the wild type, and were resistant to lysozyme. They were, however, more sensitive than the wild type to phenol, chloroform, and hypochlorite but more resistant to diethylpyrocarbonate. In all cases, resistance or sensitivity to these reagents was restored by introducing a clone of the cot alpha gene into the mutant. Since Cot alpha is an abundant outer spore coat protein of the B. cereus group with a prominent role in spore resistance and sensitivity, it is a promising target for the inactivation of B. anthracis spores.
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PMID:Characterization of a major Bacillus anthracis spore coat protein and its role in spore inactivation. 1506 44

In the context of this study, the noncovalent binding of selected phenolic compounds (chlorogenic, ferulic, and gallic acids, quercetin, rutin, and isoquercetin) to different proteins (human serum albumin, bovine serum albumin, soy glycinin, and lysozyme) was studied with direct (Hummel-Dreyer/size exclusion chromatography) and/or indirect methods (fluorescence absorbance properties of the binding components). In the latter case, the measurement of the phenol binding was achieved by exploiting the intrinsic fluorescence emission properties of quercetin as a probe. From the data obtained, the binding constants and the number of binding sites were calculated. The binding parameters were influenced by different factors, where, e.g., increasing temperature and ionic strength as well as decreasing pH cause a diminished binding. The structures of the proteins as determined by circular dichroism indicate changes in the tertiary structure with the secondary structure remaining intact.
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PMID:Binding of selected phenolic compounds to proteins. 1588 65

Since the ability of peptidoglycan (PGN) to activate Toll-like receptor 2 (TLR2) was recently questioned, we reevaluated activation of TLR2 by PGN. Polymeric soluble or insoluble Staphylococcus aureus PGN, repurified by sodium dodecyl sulfate or phenol extraction, activated TLR2 at 0.1 to 1 or 10 mug/ml, respectively, and induced tumor necrosis factor alpha production. The TLR2 activation by PGN, but not by lipoteichoic acid, was abolished by muramidase digestion. We conclude that polymeric S. aureus PGN is a TLR2 activator.
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PMID:Staphylococcus aureus peptidoglycan is a toll-like receptor 2 activator: a reevaluation. 1604 Oct 42

The purpose of this study was to determine the effect of contact lens wear on the tear film and ocular surface of people tolerant or intolerant to contact lens wear. Twenty subjects participated; 11 tolerants and nine intolerants. Their baseline tear film (no lens wear) was analysed with a range of clinical measurements and protein analyses (lactoferrin, sIgA and lysozyme). The tests were then repeated at the end of 6h of contact lens wear during the day and while lenses were worn. Both tolerants and intolerants showed statistically significant increases in bulbar and overall conjunctival redness after 6h of lens wear. For tolerants only, there was a statistically significant increase in the tear film meniscus area (0.08 mm(2) +/- 0.04 compared to 0.14 mm(2) +/- 0.06 (p = 0.023)) and a statistically significant decrease in the non-invasive tear film break-up time (NI-TBUT; 21.3 s +/- 5.7 compared to 3.7 s +/- 4.3 (p = 0.003)) after 6h of lens wear. There were no changes in other tear film or ocular surface parameters. The protein concentration and lipid layer appearance did not change during lens wear for either population. Prior to lens wear, tolerant subjects had a statistically longer NI-TBUT, higher phenol red thread test and higher tear flow rate. After 6h of lens wear and while wearing lenses, all but NI-TBUT remained statistically different. Lens wear affected only a small number of clinical variables and 6h wear did not effect the concentration of those proteins measured in tears in this study.
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PMID:The effect of short term contact lens wear on the tear film and ocular surface characteristics of tolerant and intolerant wearers. 1649 39

Ethylammonium formate (EAF), (C2H5NH3+HCO2-), is a room-temperature ionic liquid that has a polarity similar to that of methanol (MeOH) or acetonitrile. The separation at 1 mL/min of a test mixture of vitamins or phenols on a polystyrene-divinylbenzene column using either an EAF- or MeOH-water mobile phase is similar in terms of both resolution and analysis time. Because the viscosity of EAF is higher than that of MeOH, the plate count for phenol at room temperature is lower by about a factor of 1.1-1.4 depending on the flow rate. However, van Deemter plots show that this loss in plate count at 1 mL/min can be recovered and improved from 1500 to 2400 plates by working at a slightly elevated temperature of 55 degrees C. A slower flow rate such as 0.8 mL/min can also substantially improve the plate count as compared to 1-1.5 mL/min. Log P (octanol partition coefficient) versus log k' data for a variety of neutral test solutes are again similar whether EAF or MeOH is used as the organic modifier. Resolution of certain peak pairs such as 2,4-dinitrophenol/2,4,6-trinitrophenol and p-aminobenzoate/benzoate is enhanced using EAF as compared to MeOH. One advantage of EAF is that control of retention of solutes such as water-soluble vitamins under totally aqueous mobile phase conditions is environmentally preferable for quality control applications. In addition, EAF seems to be a milder mobile-phase modifier than MeOH for certain proteins such as lysozyme.
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PMID:Comparison of ethylammonium formate to methanol as a mobile-phase modifier for reversed-phase liquid chromatography. 1660 76

Esterified milk proteins [methylated (Met) or ethylated (Et) alpha-lactalbumin (ALA), beta-lactoglobulin (BLG), and beta-casein (BCN)], unmodified native milk proteins, and native basic proteins (calf thymus histone and hen egg white lysozyme) were tested for their antiviral activity against the bacteriophage M13 and for their influence on its replication (except BCN). All esterified milk proteins showed an antiviral activity against the bacteriophage M13, proportional to the extent of esterification and, hence, to the increased basicity of the modified proteins. Antiviral activity of 100% Met-BLG disappeared after its pepsinolysis but not after its trypsinolysis. The antiviral activity of Met-BLG was much higher than that of native basic proteins (histone and lysozyme). One hundred percent Met-BLG and 73% Et-BLG inhibited the replication of bacteriophage M13 completely, whereas 60% Met-ALA inhibited phage replication partially. Calf thymus histone inhibited the replication of bacteriophage M13 at a lower extent (20%) than Met- and Et-BLG (100% inhibition). Protein concentration, pH, and concentration of the Escherichia coli culture in the preincubation medium of the virus were other factors influencing antiviral activity. Interactions of esterified proteins with the phage DNA (phenol extracted) followed the same pattern as observed during studies of the inhibition of the phage replication: Met-BLG > Et-BLG > or = Met-ALA.
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PMID:Inhibition of bacteriophage m13 replication with esterified milk proteins. 1671 99

The exosporium-defective phenotype of a transposon insertion mutant of Bacillus cereus implicated ExsY, a homologue of B. subtilis cysteine-rich spore coat proteins CotY and CotZ, in assembly of an intact exosporium. Single and double mutants of B. cereus lacking ExsY and its paralogue, CotY, were constructed. The exsY mutant spores are not surrounded by an intact exosporium, though they often carry attached exosporium fragments. In contrast, the cotY mutant spores have an intact exosporium, although its overall shape is altered. The single mutants show altered, but different, spore coat properties. The exsY mutant spore coat is permeable to lysozyme, whereas the cotY mutant spores are less resistant to several organic solvents than is the case for the wild type. The exsY cotY double-mutant spores lack exosporium and have very thin coats that are permeable to lysozyme and are sensitive to chloroform, toluene, and phenol. These spore coat as well as exosporium defects suggest that ExsY and CotY are important to correct formation of both the exosporium and the spore coat in B. cereus. Both ExsY and CotY proteins were detected in Western blots of purified wild-type exosporium, in complexes of high molecular weight, and as monomers. Both exsY and cotY genes are expressed at late stages of sporulation.
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PMID:ExsY and CotY are required for the correct assembly of the exosporium and spore coat of Bacillus cereus. 1698 Apr 71

The expectorant activity of naringenin was studied. Mucus secretion was evaluated in mice by measuring the tracheal output of phenol red. Mucociliary movement function was investigated using a migration method of carbon granules in unanesthetized pigeons. And the effect of naringenin on the secretion of mucin and lysozyme was performed in the rat tracheal ring explants. Naringenin could significantly increase the secretion of phenol red from mouse tracheas at the doses of 30-67 mg/kg (i.g.) (P<0.05). Naringenin, at the dose of 90 mg/kg, increased the tracheal mucociliary velocity (TMV) to 144.4% of control (P<0.01). 100 microM naringenin could enhance the basal lysozyme secretion, but had no effect on the basal mucin secretion from the rat tracheal ring explants. Treatment with naringenin at higher concentration (10 micromol/l) could inhibit the 100 ng/ml lipopolysaccharide (LPS)-induced mucin increase. These data suggest, therefore, that naringenin has the expectorant activity.
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PMID:The expectorant activity of naringenin. 1766 77


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