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)

We used the heat denaturation of lysozyme to induce the in vitro formation of protein deposits on 60 poly-HEMA contact lenses (38.6% water). Each lens was individually placed in 20 mL of a 0.04% lysozyme solution. The lenses were divided into two equal groups. In the first group (30 lenses), bendazac lysine (100 mg) was added to the lysozyme solution. The second group of lenses was used as control. Quantitative analysis of protein deposits on the lenses of both groups was carried out by a colorimetric test. In the lenses where deposit formation occurred in the presence of bendazac lysine, a mean protein level of 7.17 +/- 3.42 micrograms per lens was found; in the control group the mean value was 30.6 +/- 8.22 micrograms per lens. Student's t-test showed this difference to be significant (P less than 0.001).
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PMID:Use of bendazac lysine to limit protein deposition on soft contact lenses in vitro. 204 21

The effects of the polycations poly-L-arginine, poly-L-lysine, and poly-ethyleneimine on rabbit neutrophil membrane permeability were compared. LDH release, quin2 release from quin2-loaded cells, and increase of indo 1 fluorescence were considered as measures for changes in membrane permeability. All polycations cause abundant LDH release. Quin2 release occurs more rapidly than LDH release, and the increase of indo 1 fluorescence is even faster. Apparently polycation-induced permeability changes occur gradually, allowing the influx (or efflux) of small molecules more rapidly than larger ones. A number of divalent and trivalent cations inhibit polycation-induced LDH and quin2 release in a way that resembles the inhibition of other cytotoxic agents described in literature. In the absence of extracellular Ca2+, the polycations induce little lysozyme release. In the presence of extracellular Ca2+, there is abundant lysozyme release, indicating that the influx of Ca2+ causes exocytosis. Exocytosis still occurs when Ca2+ is added some time after polycation addition, indicating that polycation treatment leaves the cells largely intact. All polycations tested have in common that they cause gradual changes in the permeability of the plasma membrane only, which opens the possibility to use them as membrane-permeabilizing agents for the study of Ca(2+)-induced exocytosis.
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PMID:Changes of plasma membrane permeability in neutrophils treated with polycations. 207 Nov 91

Polycationic polymers have been noted for their effects in promoting cell adhesion to various surfaces, but previous studies have failed to describe a mechanism dealing with this type of adhesion. In the present study, three polycationic polymers (chitosan, poly-L-lysine, and lysozyme) were tested for their effects on microbial hydrophobicity, as determined by adhesion to hydrocarbon and polystyrene. Test strains (Escherichia coli, Candida albicans, and a nonhydrophobic mutant, MR-481, derived from Acinetobacter calcoaceticus RAG-1) were vortexed with hexadecane in the presence of the various polycations, and the extent of adhesion was measured turbidimetrically. Adhesion of all three test strains rose from near zero values to over 90% in the presence of low concentrations of chitosan (125 to 250 micrograms/ml). Adhesion occurred by adsorption of chitosan directly to the cell surface, since E. coli cells preincubated in the presence of the polymer were highly adherent, whereas hexadecane droplets pretreated with chitosan were subsequently unable to bind untreated cells. Inorganic cations (Na+, Mg2+) inhibited the chitosan-mediated adhesion of E. coli to hexadecane, presumably by interfering with the electrostatic interactions responsible for adsorption of the polymer to the bacterial surface. Chitosan similarly promoted E. coli adhesion to polystyrene at concentrations slightly higher than those which mediated adhesion to hexadecane. Poly-L-lysine also promoted microbial adhesion to hexadecane, although at concentrations somewhat higher than those observed for chitosan. In order to study the effect of the cationic protein lysozyme, adhesion was studied at 0 degree C (to prevent enzymatic activity), using n-octane as the test hydrocarbon. Adhesion of E. coli increased by 70% in the presence of 80 micrograms of lysozyme per ml. When the negatively charged carboxylate residues on the E. coli cell surface were substituted for positively charged ammonium groups, the resulting cells became highly hydrophobic, even in the absence of polycations. The observed "hydrophobicity" of the microbial cells in the presence of polycations is thus probably due to a loss of surface electronegativity. The data suggest that enhancement of hydrophobicity by polycationic polymers is a general phenomenon.
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PMID:Mechanism of enhancement of microbial cell hydrophobicity by cationic polymers. 221 2

Seven cationic substances--human and egg-white lysozyme, RNase, protamine, histone, poly-L-lysine and poly-L-arginine; five cationic lysosomal fractions from human polymorphonuclears (PMNs); RNA; poly-L-glutamic acid; DNA; heparin; endotoxin; mastocytotropic agent compound 48/80; and cytochalasin B were tested for the influence on chemotaxis and random migration of human PMNs using under-agarose migration and Boyden chambers with two filters and [51Cr]PMNs. The above substances were either preincubated with PMNs, added to chemoattractants, or used instead of chemoattractants. In under-agarose migration method chemotaxis was inhibited by 11-35% when egg-white lysozyme, protamine, heparin, endotoxin, or compound 48/80 was added to the cells. High concentration of cytochalasin B inhibited chemotaxis by 73%. Cationic fractions I and V and low concentration of cytochalasin B enhanced chemotaxis by 11%, 41%, and 30%, respectively. When human and egg-white lysozyme, DNA, or cytochalasin B was added to the chemoattractants, motility of PMNs was inhibited. Cationic fractions II and V from human PMNs, when used as chemoattractants, enhanced cellular motility by 143-167%. Random migration was enhanced by heparin and inhibited by cytochalasin B and by cationic fractions from human PMNs. These findings suggest that various cationic and anionic substances and cationic fractions from human PMNs have heterogeneous influence on random migration and chemotactic activity of human PMN. Analysis relating chemotaxis to phagocytosis and to intracellular bactericidal activity (ICBA) has shown several patterns. Protamine, poly-L-lysine, poly-L-arginine, and agent compound 40/80 all inhibit chemotaxis and enhance phagocytosis and ICBA; cationic fractions II and V enhanced all three functions, whereas cytochalasin B suppressed phagocytosis and ICBA and had concentration-dependent modulatory influence on chemotaxis. It implies diverse mechanisms of action and possible impact on inflammatory reactions.
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PMID:Modulation of locomotor activity of polymorphonuclear cells by cationic substances and cationic lysosomal fractions from human neutrophils. 241 86

The adherence of [3H]thymidine-labeled Streptococcus sanguis strains to bare hydroxyapatite and to hydroxyapatite coated with a range of concentrations of lysozyme, poly-L-lysine, poly-L-glutamic acid, whole saliva supernatant, and combinations of some of the above was studied. Adherence of several strains of S. sanguis to bare hydroxyapatite and saliva-coated hydroxyapatite was compared. Saliva present as a pellicle on the hydroxyapatite inhibited adherence of some strains (903, M-5, 73X11) and stimulated that of others (S35, B-4, 66X49). Strains 903 and S35 were chosen for further study. Adherence of both strains was stimulated up to fivefold by the presence of adsorbed lysozyme or poly-L-lysine on the hydroxyapatite, whereas poly-L-glutamic acid inhibited adherence (80 to 95%). Adherence of strain S35 to hydroxyapatite coated with combinations of saliva and (i) lysozyme, (ii) poly-L-lysine, or (iii) poly-L-glutamic acid was unaffected compared with adherence to hydroxyapatite coated with saliva alone. In contrast, adherence of strain 903 to hydroxyapatite coated with combinations of saliva and either lysozyme or poly-L-lysine was inhibited up to ca. 90% compared with hydroxyapatite coated with saliva alone. Strain 903 was also unaffected by combinations of poly-L-glutamic acid and saliva on the hydroxyapatite. Adherent cells of both strains were completely (greater than 90%) eluted with high-ionic-strength buffer from either bare hydroxyapatite or hydroxyapatite coated with lysozyme alone. Adherent cells of strain S35 were only poorly eluted (25%) from hydroxyapatite coated with either saliva alone or saliva and lysozyme. Strain 903 elution from hydroxyapatite coated with either saliva alone or saliva and lysozyme was essentially complete. These observations were taken to indicate that the two test strains adhered to saliva-coated hydroxyapatite by different mechanisms. Protein-coated hydroxyapatite was shown not to be saturated under the conditions described here. Examination by sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the variously supplemented salivary pellicles formed on the hydroxyapatite demonstrated that major changes in salivary protein composition did not occur when lysozyme, poly-L-lysine, or poly-L-glutamic acid was used to supplement saliva. Lysozyme-dependent aggregation of strain 903 was shown not to occur under the conditions of our experiments. We suggest that the basis for stimulation of adherence to hydroxyapatite coated only with lysozyme is an increase in the cationic surface area available for electrostatic adherence of the microorganisms.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Adherence of Streptococcus sanguis to hydroxyapatite coated with lysozyme and lysozyme-supplemented saliva. 241 51

To analyze the nature of cell-cell interactions in chondrogenesis, two cations that influence these interactions, calcium and poly-L-lysine (PL), were tested for their effects on chondrogenesis in vitro. High density cultures of chick limb bud mesenchyme (Hamilton-Hamburger stages 23/24), were exposed to culture media containing calcium (0.6-3.3 mM) or PL (1-10 micrograms/ml). Both cations stimulated chondrogenesis in a dose-dependent manner, and also promoted cartilage formation in normally non-chondrogenic, low cell density cultures. Chondrogenesis was assayed based on cartilage nodule number, [35S]sulfate incorporation, and expression of type II collagen as detected by immunohistochemistry. The calcium effect was not mimicked by other divalent cations (Cd, Co, Ni, Mg, Mn, and Sr). The effect of PL was dependent on its Mr (greater than or equal to 14K) and charge, and was mimicked by poly-D-lysine but not by lysine or other analogs of PL or lysine (epsilon-amino caproic acid, lysozyme, poly-L-arginine, and spermidine). Calcium and PL probably act by different mechanisms since their effects were additive, and required their presence on different days of culture: calcium acted on Day 1, and PL on Day 2. It is proposed that calcium may play a role in the cell aggregation phase of chondrogenesis whereas PL, or a naturally occurring polypeptide of similar nature, may promote chondrogenesis by crosslinking specific anionic components of the cell surface or extracellular matrix.
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PMID:Chondrogenesis of limb bud mesenchyme in vitro: stimulation by cations. 242 99

A relatively high complexation affinity has been found for coomassie blue G-250 and the following amino acids: arginine; tyrosine; lysine; and histidine. A linear relationship was observed between log molar absorptivity and log molecular weight of 52 of 69 proteins, polypeptides, and di- and tripeptides that were allowed to react with coomassie blue G-250 in solution. The solution complexation results were used in a study of the detection of the following model proteins: bovine serum albumin, lysozyme, recombinant DNA derived human insulin, and calmodulin. Interactions between coomassie blue stained gels and silver detection reagents were determined and used as the basis for studies of enhanced sensitivity of detection of electrophoretically developed proteins. Sensitivity enhancements of up to eight-fold were observed when various sulfonic acid dye complexed proteins were detected with silver reagents versus the use of silver reagents alone. A site-directed nucleation of silver caused by the protein complexed sulfonic acid dyes is proposed as a mechanism for the observed enhancements.
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PMID:Mechanism studies of coomassie blue and silver staining of proteins. 243 Nov 34

The number and distribution of lysozyme and S100 immunoreactive cells were analyzed in ten cases of lymph node sarcoidosis. Three phases of granuloma development could be differentiated, each showing a typical immunohistological pattern. The early small granulomas consisted of lys- or very weakly lys+ mononuclear phagocytes and developed within an area of focalized accumulation of S100+ antigen-presenting cells. The mature large granulomas were composed of polygonal epithelioid cells with abundant cytoplasm showing very strong granular lysozyme positivity. S100+ cells could still be observed, mainly around the granulomas, but in diminished number. In the final fibrozing phase the epithelioid cells lost their lysozyme immunoreactivity and no S100+ antigen-presenting cells were present within or around the granulomas. In one patient granulomas with central necrosis and palisading, lys- epithelioid cells were also observed, possibly representing a different microenvironment (antigen/antibody equilibrium?). The change in the pattern and number of lysozyme and S100 immunoreactive cells probably reflects the development of the granulomas and is related to the activity of the disease.
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PMID:The distribution of S100 and lysozyme immunoreactive cells in the various phases of granuloma development in sarcoidosis. 243 36

Normal adult dogs were given intravenously lysine hydrochloride to abolish renal tubular reabsorption. The treatment caused tubular proteinuria. Once forced diuresis was established, fractional clearances for amylase, lipase, and lysozyme increased five-, 18-, and 857-fold over the baseline values, respectively. There was relatively little tubular reabsorption of amylase, and urinary amylase activity remained low. A renal arteriovenous difference in amylase activity was not present. Urinary amylase activity could not be reactivated by the addition of serum or treatment with dithiothreitol. Urinary inhibitors of amylase activity were not detected. Immunoreactive urinary amylase did not exceed kinetically measured urinary amylase. Therefore, the presence of irreversibly inactivated amylase did not explain the low fractional clearance of amylase. A small amount of serum macroamylase was present, but macroamylasemia did not account for canine amylase failing to pass the glomerular filter. It appears that the renal loss of amylase in the dog is not an important excretory route.
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PMID:Renal disposition of amylase, lipase, and lysozyme in the dog. 246 6

The influence of a soluble anionic polymer on electrophoresis of proteins was studied in relation to the nonspecific ionic effect of an affinophore on application to affinophoresis. Zone electrophoresis of proteins was carried out in agarose gel in the presence of succinyl-poly-L-lysine (degree of polymerization, 120) by using three electrophoresis buffers differing in ionic strength (0.06, 0.12 and 0.18) and pH (7.0 and 7.9). Proteins migrated as distinct single bands even in the presence of the polymer. The mobility of cationic proteins towards the cathode was first decreased and then increased towards the anode as the polymer concentration increased, while that of anionic proteins was not affected. The dependence of the apparent mobility changes of the proteins on the concentration of the polymer was treated quantitatively in the same way as affinity electrophoresis. The extent of the ionic interaction between a cationic protein and the polymer could be estimated as an apparent dissociation constant. It greatly depended on the ionic strength of the electrophoresis buffer. Except for the extremely cationic proteins such as lysozyme, the ionic interaction with up to 0.1 mM of the polymer could be practically suppressed by the use of 0.1 M sodium phosphate buffer (pH 7.0).
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PMID:Influence of a soluble anionic polymer on the electrophoresis of proteins. 247 57


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