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)

Mediators released from injured human skin that initiate the inflammatory response have not been adequately identified. Organ culture of full-thickness skin explants enables us to do so, because injury to the skin can be made in vitro, eliminating the rapid leakage of serum and infiltration of leukocytes that occur in vivo. In our studies, the military vesicant sulfur mustard (SM) (10 microliters of a 0.01 to 1.0% dilution) was topically applied to injure the epidermis of the explant. Then, the explants were cultured in small Petri dishes, usually for 18 h at 36 degrees C, and the organ-culture fluids were assayed for various inflammatory mediators. We found that the culture fluids from SM-exposed and control explants contained similar amounts of angiotensin-converting enzyme, trypsin-like and chymotrypsin-like proteases, acid phosphatase, beta-glucuronidase, beta-galactosidase, lysozyme, deoxyribonuclease, ribonuclease, interleukin 1, and lactic dehydrogenase. However, the culture fluids from SM-exposed explants contained increased amounts of histamine and plasminogen-activating activity, and often prostaglandin E2, when compared to culture fluids from control explants. After 3 to 4 d in culture, full-thickness human skin explants, when exposed to 0.2% SM (but not when exposed to 1.0% SM), sometimes showed separation of the epidermis and increased collagenase activity (i.e., hydroxyproline release). Thus, histamine (from local mast cells), and prostaglandin E2 and plasminogen-activating activity (probably from both mast cells and epidermal cells) are apparently involved in early mediation of the inflammatory response.
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PMID:Mediators, initiating the inflammatory response, released in organ culture by full-thickness human skin explants exposed to the irritant, sulfur mustard. 171 Jun 39

The previous findings that the group I and III mite allergens, and amylase present in mite faeces are hydrolytic enzymes has prompted a study to determine whether this material contains other enzymes which could be allergenic. Thus, spent growth medium devoid of whole Dermatophagoides pteronyssinus mites was shown to contain glucoamylase, lipase and lysozyme in addition to the cysteine protease, serine protease and amylase activities associated with the above allergens, respectively. All of these enzymes are probably associated with mite digestive processes. They were rapidly solubilised, heterogeneous with regard to charge (pI in the range 4-8) and demonstrated maximum biochemical activity in the neutral pH range. Three serine proteases were detected and comprised a chymotrypsin-like, a trypsin-like and an unclassified enzyme with pI of 4.1 and 5.3, 8.5 and 7.1, respectively. Only one cysteine protease was observed, which paralleled immunochemically identified Der p I in a variety of assays. It was shown to cleave at lysyl residues and could be inhibited by the specific cysteine protease inhibitor, E-64. The remaining serine proteases, glucoamylase, lipase and lysozyme represent potential allergens.
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PMID:Faecally derived hydrolytic enzymes from Dermatophagoides pteronyssinus: physicochemical characterisation of potential allergens. 171 11

Of the interactions that govern protein adsorption on polymer surfaces, solvation interactions (repulsive hydration and attractive hydrophobic interactions) are thought to be among the most important. The solvation interactions in protein adsorption, however, have not been dealt with in theoretical calculation of the adsorption energy owing to the difficulties in modelling such interactions. We have evaluated the solvation interaction energies using the fragment constant method of calculating the partition coefficients of amino acids. The fundamental assumption of this approach is that the partition coefficients of amino acids between water and organic solvent phases are related to the free energies of transfer from bulk water to the polymer surface. The X-ray crystallographic protein structures of lysozyme, trypsin, immunoglobulin Fab, and hemoglobin from the Brookhaven Protein Data Bank were used. The model polymer surfaces were polystyrene, polypropylene, polyethylene, poly(hydroxyethyl methacrylate) [poly(HEMA)], and poly(vinyl alcohol). All possible adsorption orientations of the proteins were simulated to study the effect of protein orientation on the solvation interactions. Protein adsorption on either hydrophobic or hydrophilic polymer surfaces was examined by considering the sum of solvation and other interaction energies. The results showed that the contribution of the solvation interaction to the total protein adsorption energy was significant. The average solvation interaction energy ranged from -259.1 to -74.1 kJ/mol for the four proteins on the hydrophobic polymer surfaces, such as polystyrene, polypropylene, and polyethylene. On the other hand, the average solvation interaction energies on hydrophilic surfaces such as poly(HEMA) and poly(vinyl alcohol) were larger than zero. This indicates that repulsive hydration interactions are in effect for protein adsorption on hydrophilic polymer surfaces. The total interaction energies of the proteins with hydrophobic surfaces were always lower than those with more hydrophilic surfaces. This trend is in agreement with the experimental observations in the literature. This study suggests that consideration of the solvation interaction energies is necessary for accurate calculation of the protein adsorption energies.
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PMID:Calculation of solvation interaction energies for protein adsorption on polymer surfaces. 176 35

The physiologic substrates of cytotoxic T lymphocyte granule-associated serine esterases (referred to hereafter as proteases or "granzymes"), and the role of these enzymes in cell-mediated activity remain unclear. We have developed an assay for possible ligands of the trypsin-like dimeric serine protease granzyme A based on Western immunoblotting techniques. This protein-binding assay demonstrates the selective binding of granzyme A to several proteins present in the target cell P815. The binding specificity is preserved when enzyme binding is performed in the presence of excess competing proteins, including such cationic species as lysozyme and RNase. Enzyme binding is inhibited, however, by heat or detergent inactivation of granzyme A. Subcellular fractionation of target cells shows that the nuclear fraction contains most granzyme A binding reactivity, which is recovered in the nuclear salt wash fraction. A protein with Mr = 100,000 and two closely migrating proteins with Mr = 35,000 and 38,000 are the predominant reactive moieties, and the N-terminal sequence of the 100-kDa protein confirmed that this protein was murine nucleolin. Incubation of granzyme A with nucleolin generates a discrete proteolytic cleavage product of Mr = 88,000. Since nucleolin is known to shuttle between nucleus and cytoplasm, the interaction of granzyme A and nucleolin may be important in the process of apoptosis which accompanies cytotoxic T lymphocyte-mediated lysis of target cells.
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PMID:Granzyme A binding to target cell proteins. Granzyme A binds to and cleaves nucleolin in vitro. 186 Aug 69

CD spectra of reduced and S-3-(trimethylated amino) propylated lysozyme (TMAP lysozyme) have been measured in various solutions containing guanidine hydrochloride or trifluoroethanol (TFE). The CD spectra indicate that there remain residual secondary structures in protein in aqueous solution. The addition of TFE further promotes the formation of secondary structures. In order to examine whether secondary structures are evenly induced over all the polypeptide chain, or locally at particular segments, the limited proteolysis of TMAP lysozyme by trypsin has been performed, and the CD spectra of all the final and intermediate products have been observed in solutions containing TFE. As a result, the fragments vary in a helix-forming propensity. The CD spectra of peptide fragments T5, T7, T9T10, T12T13, T14T15T16, and T17T18 are not significantly affected by the addition of TFE, where T refers to the nomenclature of R.E. Canfield [(1963), Journal of Biological Chemistry, Vol. 238, pp. 2691-2697]. They are fragments of a helix-breaking propensity. On the other hand, fragment I2 composed of T1-T4, and fragments T6T7, T8, and T11, attain secondary structures with the addition of TFE. They are fragments of a helix-forming propensity. Further, it is found that the fragments of a helix-forming propensity just correspond to the helical segments in native lysozyme. We examine the interactions between neighboring fragments, which contribute to the stabilization of local structures along the polypeptide chain.
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PMID:Local structures in unfolded lysozyme and correlation with secondary structures in the native conformation: helix-forming or -breaking propensity of peptide segments. 186 65

The article analyses the results of treatment of 150 patients with purulent diseases of the soft tissues of various localization, in which after surgical treatment the purulent focus immobilized trypsin (50 patients), trypsin with lysozyme immobilized on gauze (50 patients), and antiseptics (50 patients) were used for topical treatment of the formed wounds. The results of the treatment showed that topical prolonged enzyme therapy of purulent wounds with the use of trypsin immobilized on gauze and that with lysozyme promotes cleansing of the wounds, reduces microbial dissemination, intensifies reparative processes, and reduces the terms of treatment.
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PMID:[Prolonged local enzyme therapy of suppurative wounds]. 192 Nov 98

The antilysozyme activity of 184 meningococcal strains was studied. Such activity was found in all strains within the range 1-25 micrograms/ml, which was due to the heterogeneity of bacterial population. Strains varying in the total level of their lysozyme activity differed in the population structure by this sign. Preparations inhibiting antilysozyme activity could be differentiated according to the character of their action by the method of the population analysis. In the process of phagocytosis the selection of clones with a high level of antilysozyme activity was found to occur. The antilysozyme factor, heat resistant protein with a molecular weight of 10,000-30,000 D, was sensitive to trypsin.
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PMID:[The antilysozyme activity of meningococci]. 195 Feb 56

Pure DMSO (instead of water) is used as the reaction medium for protein separations. It is shown that common extracellular proteins (i) have high solubility in DMSO (1-50 mg/ml), (ii) do not irreversibly inactivate in this solvent, and (iii) can adsorb onto carboxymethyl cellulose in DMSO and be subsequently fully desorbed in this solvent by inorganic salts. Ion-exchange chromatography on this resin in DMSO has been used to purify bovine pancreatic trypsin and to separate it from hen egg-white lysozyme in their mixture. Another approach to protein separation in DMSO, fractional precipitation with ethyl acetate (which does not dissolve proteins), has been verified with a mixture of bovine pancreatic chymotrypsinogen and chicken egg ovalbumin.
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PMID:Protein separation and purification in neat dimethyl sulfoxide. 203 25

The bioavailability of sIgA and lysozyme from human milk was investigated in a total of 41 infants by radial immunodiffusion and by the Micrococcus lysodeicticus method, respectively. In four different pools of human milk used for balance studies the sIgA concentrations ranged between 2,200 and 17,850 mg/l. The lysozyme concentration varied from 64.5 to 283.5 mg/l. On human milk feeding the excretion of sIgA in 19 infants was 3,200 (0-8,200) mg per litre and 9.7 (0-131) mg lysozyme per litre, respectively. Corresponding values on formula feeding in 22 infants were 1030 (0-6400) and 2.6 (0-9) mg/l. Fecal sIgA excretion was significantly higher on human milk than on formula feeding. Balances of sIgA and lysozyme intake and excretion as performed in 9 infants revealed a less than 1% fecal excretion of both the protective substances. In vitro digestion of raw human milk with pepsin at pH 2 and 3 resulted in a rapid disappearance of immunologically reactive sIgA within 30 minutes after starting the incubation, while no changes in sIgA content were detectable at pH 4. Lysozyme proved to be resistant against peptic digestion. Tryptic digestion at pH 8 did not result in a decrease of human milk sIgA within 120 minutes of incubation at 37 degrees C while under analogous conditions lysozyme concentration approached to 0. These results point at the full bioavailability of both sIgA and lysozyme from human milk. The differing resistance of these protective substances against pepsin and trypsin is apparently adapted to physiological particularities of the digestive tract in early infancy.
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PMID:[Fecal sIgS and lysozyme excretion in breast feeding and formula feeding]. 211 35

Using the monoclonal antibody HAM-56 with the avidin-biotin method on recent or archival paraffin-embedded tissue from multiple sclerosis brains, we have been able to distinguish between acute, chronic active and inactive lesions. HAM-56 stains all macrophages, monocytes and at least some microglia; it is the only pan-macrophage marker to our knowledge that can be satisfactorily used on conventional paraffin sections. A much narrower range of mainly perivascular macrophages in acute plaques of multiple sclerosis is stained with MAC-387, anti-muramidase and anti-alpha1-anti-trypsin. The acute plaques show HAM-56-stained macrophages throughout the lesion, and these macrophages exhibit profiles of phospholipid-rich myelinic bodies, which are also usually stainable with Luxol fast blue. Active ongoing lesions show a rim of macrophages at the edge of the lesion. These macrophages show profiles of large vacuoles, thought to represent the sudanophilic esterified cholesterol formed during demyelination. Inactive cases show none of these features; the few perivascular macrophages present often contain the end product of lipid peroxidation, ceroidlipofuscin.
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PMID:Macrophage histology in paraffin-embedded multiple sclerosis plaques is demonstrated by the monoclonal pan-macrophage marker HAM-56: correlation with chronicity of the lesion. 214 83


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