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)

Water-soluble and 0.6 M KCl-soluble protein fractions prepared from Tetrahymena pyriformis, when inoculated into mice, could effectively induce activated macrophages having the ability to kill Toxoplasma gondii in vitro. This effect was not induced by other proteins tested, such as bovine serum albumin, pepsin from porcine stomach mucosa and chicken egg-white lysozyme, nor by muramyl dipeptide (MDP), a potent immunoadjuvant. Five fractions obtained by DEAE-Sephadex chromatography of the water-soluble protein fraction were compared with regard to induction of toxoplasmacidal activity in macrophages. The first peak was most effective for activation of macrophages. Five fractions obtained by chromatography of the 0.6 M KCl-soluble protein fraction were also examined and it was found that the first peak had the activity. No marked difference in activity was observed between the active fractions of water-soluble and 0.6 M KCl-soluble protein fractions. For practical use, we focused on the water-soluble active fraction. The minimum effective dose of the active fraction was 100 micrograms and the fraction could activate macrophages directly in vitro. Four fractions obtained by gel filtration of the active fraction on Sephadex G-200 were compared and the first peak had the activity. The first peak contained a single protein, revealed by SDS-polyacrylamide gel electrophoresis; its apparent molecular weight was 64,000.
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PMID:Macrophage activation by Tetrahymena pyriformis. II. Active protein fractions from Tetrahymena. 308 3

P388D1 is a murine macrophage cell line which spontaneously secretes plasminogen activator (PA; activated function) and lysozyme (LYS; constitutive function). Compounds which decrease PA secretion without affecting LYS secretion have potential as "down-regulators" of macrophage function and, hence, of the immune system. Glucocorticoids (e.g., dexamethasone, IC50 less than 0.01 microM) and auranofin (IC50 = 1 microM) are positive in this model. In contrast, cyclooxygenase inhibitors (indomethacin, ibuprofen and piroxicam, all at 1 microM) boost PA secretion; lipoxygenase inhibitors (REV-5901, NDGA and piriprost, all at 10 microM) have little or no effect. Dexamethasone, but not auranofin, induces a urokinase-inhibitory activity which elutes between 0.13 and 0.19 M NaCl upon anion exchange HPLC (TSK-DEAE-5-PW). Fibrin overlay following SDS-PAGE of the HPLC peak reveals a urokinase-inhibitory band at approximately 90 Kd.
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PMID:Pharmacological modulation of plasminogen activator secretion by P388D1 cell line. 312 May 14

DNA could not be quickly extracted from members of the genus Actinomyces by the usual methods of lysis. Treatment of 7 different actinomyces cells with lysozyme and achromopeptidase, both 5 mg/g wet cells, for 2 h, followed by SDS (0.2%), proteinase K (5 mg/g wet cells) and EDTA (lmM) for 1 h, lysed the cells. The yield obtained in one day was 337 micrograms per 200 mg of bacterial cells. The treatment was also found to work effectively on strains belonging to Veillonella, Staphylococcus, Fusobacterium and Bifidobacterium genera.
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PMID:Rapid isolation of DNA from Actinomyces. 312 48

Malonic dialdehyde (MDA) is produced in all mammalian tissues either as an end product of lipid peroxidation or as a by-product of arachidonic acid metabolism. It may either be quickly oxidized to carbon dioxide or combine covalently with primary amino groups of proteins, phospholipids or nucleic acids. In the latter case, fluorescent Schiff's bases with 1-amino-3-iminopropene (AIP) bridges are produced. MDA metabolism is now fairly well elucidated, while that of MDA-cross-linked biological molecules remains unknown. Aiming at investigating the fate of such cross-linked molecules in mammalian organisms, and their biological relevance, we tried in the present study to prepare reproducibly Schiff's bases from chicken egg white lysozyme reacted with MDA. The resulting mixture of different Schiff's bases (ML) was fractionated into single oligomeric fractions by gel-filtration chromatography. ML and the single oligomeric fractions obtained from this mixture were controlled by fluorescence measurements for their content of AIP bridges, and by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate (SDS-PAGE) for their content of different oligomers. ML contained monomers, dimers, trimers and other oligomers, as shown by SDS-PAGE. The corresponding single oligomeric fractions were satisfactorily separated by gel-filtration chromatography (purity better than 94%, as determined by SDS-PAGE). Schiff's bases from poly-L-lysine reacted with MDA (MP) were also prepared. Their fluorescence emission spectrum was similar to that of ML and to that of the single oligomeric fractions obtained from ML.
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PMID:Immunological relevance of malonic dialdehyde. I. Preparation of Schiff's bases from lysozyme or polylysine reacted with malonic dialdehyde. 312 19

Antibodies were raised against purified germination-specific cortex-lytic enzyme (GSLE) from spores of Bacillus megaterium KM which neutralized the ability of GSLE to germinate permeabilized spores. Western blotting of dormant spore and vegetative cell fractions separated by SDS-PAGE demonstrated that GSLE is spore-specific and that greater than 90% of the GSLE is associated with the dormant spore cortex peptidoglycan as a phosphorylated 63kD pro-form, which could only be visualized after lysozyme digestion of the peptidoglycan. During germination, the 63kD pro-form of GSLE is processed to release the active enzyme, which had an apparent molecular weight of 30kD. Inhibitor studies demonstrated that GSLE activation occurs as part of the commitment reaction and thus represents the first-identified enzymatic event to occur during germination triggering. Proteins that cross-react with anti-GSLE sera are present in spore fractions of other species.
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PMID:Germination-specific cortex-lytic enzyme is activated during triggering of Bacillus megaterium KM spore germination. 314 85

Alkaline phosphatase activity in mouse liver blocks, cooled by an ice-bath, decreased by 50% in 5 min of microwave irradiation (280 W). This loss of protein tertiary structure has been mirrored by ultrastructural changes in the same tissue. Microwave irradiation did not produce cleavage or polymerization of lysozyme or haemoglobin. Protein formaldehyde reaction mixtures produced protein polymers between 0 degree and 40 degrees C which could be separated by SDS-polyacrylamide gel electrophoresis. Microwave irradiation of lysozyme or haemoglobin plus formaldehyde on ice-bath up to 30 min produced a similar electrophoretic pattern. When lysozyme or haemoglobin plus formaldehyde was heated to 60 degrees C for 30 min, the protein polymers migrated faster on electrophoresis, suggesting a smaller hydrodynamic volume than expected due to intramolecular crosslink formation, not opened up under the conditions of electrophoresis.
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PMID:Differentiating the effects of microwave and heat on tissue proteins and their crosslinking by formaldehyde. 322 Jul 96

Lysozyme can be separated commercially from other egg components and is used as a natural, antibiotically active protein. A method for the detection of de-lysozymed egg products using SDS-polyacrylamide gel electrophoresis (PAGE) is described. The method can also be used for lysozyme quantification. Lysozyme concentrations in egg products are tentatively assigned to three classes, based on the lysozyme contents found in intact eggs. The results obtained from a series of egg products on the market allow two groups to be distinguished. The first group has values for average lysozyme content, standard deviation and total protein content very close to the values found for intact eggs, and the second group clearly shows a lower lysozyme content but a total protein content comparable with intact eggs.
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PMID:Determination of lysozyme content in eggs and egg products using SDS-gel electrophoresis. 322 94

Human polymorphonuclear leucocytes (PMNs) will phagocytose yeasts opsonized with specific affinity-purified human serum IgA. PMNs also bind to Sepharose beads coated with IgA or IgG, but not to beads coated with bovine serum albumin (BSA) or horseradish peroxidase (HRP). Binding to IgA-Sepharose stimulates the cells to release lysozyme. Affinity chromatography of 125I-labelled PMN membrane proteins on IgA-Sepharose results in isolation of a polypeptide of apparent 60,000 MW. The protein, which is not bound to IgG-Sepharose under the same conditions, appears as a diffuse band on SDS-PAGE, suggesting it is heavily glycosylated.
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PMID:Characterization of the IgA receptor from human polymorphonuclear leucocytes. 329 6

The glycoconjugate composition of tracheal secretions varies with physiological and pathophysiological parameters. Believing that these differences might be explained by metabolic or regulatory modifications of particular cell types, we have developed strategies for biochemical analysis at the cellular level. We have produced monoclonal antibodies whose determinants are restricted to a single secretory cell type (serous, mucous, or goblet cell granules, or ciliated cell glycocalyx). By enzyme immunoassay (ELISA), we have characterized four of the antibodies biochemically, and have also used the antibodies as quantitative molecular probes to detect release of antigen from mixed cell explants. Four of the antigens are carried by carbohydrate moieties of high molecular weight glycoproteins. Western blot analysis shows their molecular weight in reducing gels (SDS-PAGE) to exceed 200 kD. When used in parallel with pulse-chase labeling studies, the antibodies are both more sensitive and specific (than bound radioactivity) in detecting gland or goblet cell secretion in response to autonomic drugs or proteases. We have also isolated and cultured serous gland cells for physiological and biochemical studies. These cells express serous cell phenotype as reflected by ultrastructure, histochemistry, and lysozyme activity. Biochemical analysis of their secretory products reveals glycoconjugate components which are heterogeneous with respect to both molecular weight and charge. Radiolabeled secretory products eluting in the void volume of Sepharose C1 4B were completely degraded by chondroitinase ABC. This indicates that the major glycoconjugate produced by serous cell is a proteoglycan resembling chondroitin sulfate.
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PMID:Studies of tracheal secretion using serous cell cultures and monoclonal antibodies. 350 59

Wild-type T4 lysozyme contains unpaired cysteine residues at positions 54 and 97. To investigate the role these residues play in the thermal inactivation of the wild-type, we constructed a double mutant with these cysteines replaced with valine and serine. This molecule, T4 lysozyme (C54V/C97S), is more stable than the wild-type to inactivation at 70 degrees C at pH 6.5 and 8.0. Guanidine hydrochloride reactivation experiments and SDS-PAGE on the inactivated products show that the wild-type is susceptible to varying degrees of oxidative damage, depending on buffer conditions, while the cysteine-minus mutant inactivates only by other pathways. The products of thermal, oxidative inactivation of the wild-type are disulfide-linked oligomers. The dependence of inactivation rate on temperature suggests that the formation of these aggregates depends on prior thermal unfolding of the T4 lysozyme molecule.
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PMID:The role of cysteine oxidation in the thermal inactivation of T4 lysozyme. 350 92


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