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)

We investigated and compared the initial composition, morphology, and time course of deposits on individual soft contact lenses of different water contents and surface charges in order to evaluate the potential for antigenic reactions and to predict the optimal frequency of lens replacement. Newly manufactured lenses were worn for graduated periods of time from 1 min to 8 h by subjects who were first adapted to daily wear soft lenses. The morphology and composition of the deposits were analyzed by histological staining, light microscopy, scanning electron microscopy (SEM), sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) with silver nitrate staining, and immunofluorescence microscopy. The protein bands of the acrylamide gels were divided according to their molecular weights into six groups which have been defined in the literature from tear analyses by electrophoretic techniques and include lysozyme, proteins migrating faster than albumin (PMFA), protein G, albumin, lactoferrin, and other proteins heavier than albumin such as Ig-G and secretory Ig-A. Specific proteins (lysozyme, PMFA, and protein G) were detected on individual lenses after as little as 1 min of wear. There was an increasing amount of protein deposited as the wearing time increased. Differences in the rates and amounts of deposition were more dependent on lens water content and ionic characteristics than on intersubject differences. Such early significant protein deposition may occur in wearers of disposable lenses as well as in those subject to complications due to accumulation of protein.
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PMID:Initial in vivo tear protein deposition on individual hydrogel contact lenses. 220 14

Refinement of triclinic lysozyme by restrained least squares against the 2 A resolution X-ray data is described, beginning with the model from cycle 17 of the preceding paper [Hodsdon, Brown, Sieker & Jensen (1990). Acta Cryst. B46, 54-62]. After 20 refinement cycles, R stood at 0.172. Nevertheless, serious errors involving both main-chain and side-chain atoms still remained, requiring numerous model rebuilding sessions interleaved with refinement cycles. After 63 cycles R = 0.124 for the model which includes all protein atoms, 249 water oxygen sites and five nitrate ions. Although the overall B is relatively low, 10.5 A2, B's for atoms in the region of residues 101-103, toward the termini of some of the longer side chains, and in the region of the C terminus of the main chain exceed 20 A2, indicating relatively high atomic mobilities, disorder, or remaining errors in the model.
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PMID:Refinement of triclinic lysozyme: II. The method of stereochemically restrained least squares. 230 27

Crystallization conditions for hen egg white lysozyme in the presence of various ions were determined at pH 4.5 and 18 degrees C. The corresponding solubility curves show that the main effects are due to anions in the following order: SCN- greater than NO3- greater than Cl- greater than citrate2- greater than CH3COO- approximately H2PO4- greater than SO4(2-). This is in the reverse order of the lyotropic series of Hofmeister. As a consequence, SCN- precipitates and crystallizes lysozyme at low concentration, whereas sulfate is ineffective even at high concentrations. Crystals obtained with each salt were characterized by x-ray diffraction. Lysozyme thiocyanate and nitrate crystals belong to the monoclinic system, whereas all the others have a tetragonal lattice.
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PMID:Relative effectiveness of various ions on the solubility and crystal growth of lysozyme. 291 Aug 63

Thirty strains were isolated from pasteurized soil samples by enrichment culture in aerobiosis at 32 degrees C in a minimal medium containing one of the following compounds as sole source of carbon and energy: quinate, p-hydroxybenzoate, phthalate, isophthalate or trimellitate. These bacteria were rods (0.8 X 2-7 micron), motile by peritrichous flagella. Endospores were oval (1.4-1.8 X 2 micron) and distinctly swelled the sporangia. The Gram reaction was variable but the Gram type was positive. Colonies were smaller on peptone (0.4%) agar than on minimal salts-glucose (0.2%) agar. The following characters were always present: growth in the presence of lysozyme, cytochrome c oxidase, catalase, nitrate assimilation, urease, amylase and L-glutamate dehydrogenase. The cells contained glycogen. In anaerobiosis, glucose was not fermented and nitrate was not used as a respiratory acceptor of electrons. Of 215 substrates tested, 31 (including 9 aromatic compounds) were used as sole carbon and energy sources by all 30 strains, and 38 substrates (including 13 aromatic compounds) were used by only some of them; 146 substrates (including 49 aromatic compounds) were not used by any of the 30 strains. No amino acid could be used as sole carbon and energy source. Numerical analysis of the 30 strains showed an aggregate cluster made of 5 phena. The mean G + C content of the DNA was 55 +/- 0.6 mol %. The described bacteria are clearly different from the 2 known species of the second morphological group which cannot ferment carbohydrates: Bacillus brevis and B. azotoformans. Strain Q1 (ATCC 29948) is the holotype of Bacillus gordonae sp. nov.
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PMID:[Bacillus gordonae sp. nov., a new species belonging to the second morphological group, degrading various aromatic compounds]. 367 81

Legionella pneumophila, the etiologic agent of Legionnaires' disease, is phagocytized in an unusual way and multiplies in human mononuclear phagocytes in a novel phagosome. As a first step toward understanding these L. pneumophila-phagocyte interactions, we have studied the envelope of L. pneumophila Philadelphia 1 strain. We isolated cell envelopes by treating whole bacterial cells with lysozyme and EDTA to convert them to spheroplasts, then lysing the spheroplasts osmotically or sonically. We resolved the cell envelopes into two membrane fractions by isopycnic centrifugation. We localized NADH oxidase to the fraction of buoyant density 1.145, which we designated cytoplasmic membrane, and lipopolysaccharide (LPS) to the fraction of density 1.222, which we designated outer membrane. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) revealed that the L. pneumophila outer membrane contains a single major protein species migrating at 28,000 mol wt; this is the major protein of the bacterium. The cytoplasmic membrane also contains a single major protein species migrating at 65,000 mol wt. Surface iodination of the bacteria and agglutination and immunofluorescence studies with rabbit antibody produced against the purified major outer membrane protein (MOMP) revealed that this protein is exposed at the cell surface. We isolated LPS from L. pneumophila membranes by SDS-EDTA treatment. The pattern obtained by subjecting the LPS to SDS-PAGE and staining the gel with silver nitrate suggests that L. pneumophila LPS might be atypical. We studied patient serologic responses to cell envelope components of L. pneumophila Philadelphia 1, a serogroup 1 organism. Sera from patients with evidence of infection with serogroup 1 L. pneumophila contained large amounts of antibody to this strain. Few of these antibodies recognized the MOMP of L. pneumophila. In contrast, greater than 98% of these antibodies were directed against the LPS. This indicates that LPS is the dominant serogroup antigen and the major antigen responsible for the reactivity of patient sera in the indirect fluorescent antibody assay, currently the principal diagnostic assay for Legionella infection.
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PMID:Isolation and characterization of the cytoplasmic and outer membranes of the Legionnaires' disease bacterium (Legionella pneumophila). 388 79

Membranes were isolated from Bacillus stearothermophilus 2184D by lysozyme digestion of the cell wall and subsequent differential centrifugation. Observations with the electron microscope indicate that such membranes are relatively intact and have a typical membrane appearance. Nitrate will preferentially oxidize the cytochrome b of such membranes. Approximately 80% of the total respiratory nitrate reductase activity of whole cells can be localized in the washed membrane fraction and the process of membrane isolation results in a sixfold purification of this enzyme. Of several detergents tested, sodium dodecyl sulfate, Triton 114, and Triton X-100 are most effective in converting reduced methyl viologen-nitrate reductase to a form which will not pellet at 130,000 x g. Density gradient analysis reveals that such detergent-mediated solubilization converts virtually all membrane protein to a form of lighter density.
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PMID:Localization and solubilization of the respiratory nitrate reductase of Bacillus stearothermophilus. 433 9

Six synthetic antimicrobial steroids were examined for indications of their mechanism of action. Dequadin acetate, cetyl pyridinium chloride (CPC), and sodium deoxycholate were studied for comparison. Aerated cells of Sarcina lutea were washed, suspended in 1.06 M sucrose, and converted to protoplasts with 20 mug/ml of lysozyme. Lysis was measured optically at 650 mmu as a decrease in optical density. Screening tests with 50 mug/ml of each compound showed five steroids and CPC to be lytic. Protoplasts were strongly protected from lysis by pretreatment with 0.001 to 0.004 M spermine tetrahydrochloride. Other polyamines, such as spermidine phosphate, were less protective, and putrescine was ineffective. Uranyl nitrate (5 x 10(-4) M) rapidly agglutinated protoplasts and protected them from rupture by the lytic agents. Similar studies with 0.001 to 0.004 M Mg(++) showed varying degrees of protection, which, in most cases, was only temporary. Steroidal lysis did not appear to be related to chelation, since ethylenediaminetetraacetate did not cause lysis alone and antagonized some lytic compounds. Lecithin, Tween 80, Tween 20, and Span 20 at 0.05% exhibited certain effects on protoplast stability. Span 20 strongly prevented lysis by steroids. Tween 20 alone quickly caused protoplast rupture. Lecithin and Tween 80, which also caused lysis alone, interfered with lytic steroids and CPC. The test compounds were both inhibitory and lethal to cells of Sarcina lutea. The results suggest that direct action on cell membranes may be chiefly responsible for the antimicrobial properties of the steroids.
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PMID:Steroid lysis of protoplasts and effects of stabilizers and steroid antagonists. 495 42

All of the common cytochalasins activate superoxide anion release and exocytosis of beta-N-acetylglucosaminidase and lysozyme from guinea-pig polymorphonuclear leukocytes (neutrophils) incubated in a buffered sucrose medium. Half-maximal activation of both processes is produced by approx. 0.2 microM cytochalasin A, C greater than 2 microM cytochalasin B greater than or equal to 4-5 microM cytochalasin D, E. While maximal rates of O2- release and extents of exocytosis require extracellular calcium (1-2 mM), replacing sucrose with monovalent cation chlorides is inhibitory to neutrophil activation by cytochalasins. Na+, K+ or choline inhibit either cytochalasin B- or E-stimulated O2- production with IC50 values of 5-10 mM and inhibition occurs whether Cl-, NO3- or SCN- is the anion added with Na+ or K+. Release of beta-N-acetylglucosaminidase in control or cytochalasin B-stimulated cells is inhibited by NaCl(IC50 approximately 10 mM), while cytochalasin E-stimulated exocytosis is reduced less and K+ or choline chloride are ineffective in inhibiting either cytochalasin B- or E-stimulated exocytosis. Release of beta-glucuronidase, myeloperoxidase or acid phosphatase from neutrophils incubated in buffered sucrose is not stimulated by cytochalasin B. Stimulation of either O2- or beta-N-acetylglucosaminidase release by low concentrations of cytochalasin A is followed by inhibition of each at higher concentrations. It appears that all cytochalasins can activate both NAD(P)H oxidase and selective degranulation of neutrophils incubated in salt-restricted media and that differential inhibition of these two processes by monovalent cations and/or anions is produced at some step(s) subsequent to cytochalasin interaction with the cell.
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PMID:Activation of superoxide production and differential exocytosis in polymorphonuclear leukocytes by cytochalasins A, B, C, D and E. Effects of various ions. 627 16

1. A method is described for preparing spheroplasts from Paracoccus denitrificans that are substantially depleted of dissimilatory nitrate reductase (cytochrome cd) activity. Treatment of cells with lysozyme + EDTA together with a mild osmotic shock, followed by centrifugation, yielded a pellet of spheroplasts and a supernatant that contained d-type cytochrome. The spheroplasts were judged to have retained an intact plasma membrane on the basis that less than 1% of the activity of a cytoplasmic marker protein, malate dehydrogenase, was released from the spheroplasts. In addition to a low activity towards added nitrite, the suspension of spheroplasts accumulated the nitrite that was produced by respiratory chain-linked reduction of nitrate. It is concluded that nitrate reduction occurs at the periplasmic side of the plasma membrane irrespective of whether nitrite is generated by nitrate reduction or is added exogenously. 2. Further evidence for the integrity of the spheroplasts was that nitrate reduction was inhibited by O2, and that chlorate was reduced at a markedly lower rate than nitrate. These data are taken as evidence for an intact plasma membrane because it was shown that cells acquire the capability to reduce nitrate under aerobic conditions after addition of low amounts of Triton X-100 which, with the same titre, also overcame the permeability barrier to chlorate reduction by intact cells. The close relationship between the appearance of chlorate reduction and the loss of the inhibitory effect of O2 on nitrate reduction also suggests that the later feature of nitrate respiration is due to a control on the accessibility of nitrate to its reductase rather than on the flow of electrons to nitrate reductase.
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PMID:The location of dissimilatory nitrite reductase and the control of dissimilatory nitrate reductase by oxygen in Paracoccus denitrificans. 719 18

Streptococcus mutans BHT was grown in a synthetic medium containing radioactive thymidine to monitor deoxyribonucleic acid release. Kinetic experiments demonstrated that although lysozyme alone could not liberate deoxyribonucleic acid, cellular deoxyribonucleic acid was liberated from lysozyme-treated cells by addition of low concentrations of inorganic sodium salts. When the salts were tested for their ability to dislodge cell-bound tritiated lysozyme, the extent of the initial release of enzyme by individual anions correlated with the anion potency for deoxyribonucleic acid liberation (SCN- greater than ClO4- greater than I- greater than Br- greater than NO3- greater than Cl- greater than F-), although the total amount of lysozyme dislodged did not correspond directly with cell lysis. Differences in the effectiveness of anions (SCN-, HCO3-, Cl- and F-) in potentiating cell lysis could be enhanced or minimized by varying the lysozyme, anion, and bacterial cell concentrations. As the anion concentration was increased for each enzyme concentration and cell concentration, the lysis increased, in some cases markedly, until maximum levels of released deoxyribonucleic acid were attained. The maximum levels of lysis of SCN- and HCO3- were similar and were greater than those for Cl- and F-. In addition, the maximum levels were observed to increase for each of the anions as the concentration of lysozyme increased.
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PMID:Lysis of Streptococcus mutans by hen egg white lysozyme and inorganic sodium salts. 721 17


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