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)

Immunostaining paraffin sections of appropriately fixed tissues with an antiserum to human urinary lysozyme as the primary step in an immunoglobulin-peroxidase bridge method has localized lysozyme in previously recognized sites such as Paneth cells, renal tubules, and lymph node macrophages in several species. In addition, lysozyme was demonstrated in the ciliary layer of the trachea, and type II pneumocytes, as well as cells of presumed mucoid nature in laryngotracheal glands. Large stellate cells in follicle centers in the lymph nodes and spleen and in the medulla of the thymus evidenced strong lysozyme reactivity. Granular pneumocytes disclosed immunoreactivity for lysozyme also at the ultrastructural level. Lysoplate assay demonstrated lysozyme in abundance in both the cellular pellet and acellular supernatant of rat alveolar wash fluid and in rat lung after repeated washing of alveoli. Hamster lung differed from the others in failing to immunostain for lysozyme and affording no evidence for content of lysozyme as determined by lysoplate assay. Sites stained with antiserum to human urinary lysozyme failed to stain with antiserum to egg white lysozyme. However, the pyloric glands, Golgi elements in intestinal epithelium, the surface of the colon, and the proximal straight renal tubule of the mouse stained exclusively with the antiserum to hen egg white lysozyme. Many sites staining with antiserum to urinary lysozyme in respiratory, renal, and lymphoid tissue lacked reactivity in control sections exposed to this antiserum after it was absorbed with purified urinary lysozyme. However, mucous acini in submandibular glands, although failing to stain with other control procedures, retained towared the absorbed antiserum, possibly through reacting with an antibody other than that for human urinary lysozyme. A number of cell types containing proteinaceous cytoplasmic granules stained in control sections exposed to normal serum in place of antilysozyme serum in the immunoglobulin-peroxidase bridge procedure and, thus, possessed selective, but nonimmunospecific affinity for immunoglobulin. Cell types that stained with antiserum to hen egg white lysozyme lost affinity for the antiserum after its absorption with egg white lysozyme but retained the affinity after absorption with urinary lysozyme.
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PMID:Immunocytochemical localization of lysozymes in respiratory and other tissues. 32 Mar 84

Phorbol myristate acetate (PMA, 2 to 100 ng/ml) and ionophore A23187 (10(-7) to 10(-6) M) cause human neutrophils to release up to 50% of the granule-associated enzyme lysozyme extracellularly without release of beta-glucuronidase or the cytoplasmic enzyme LDH. When azurophil and specific granules are separated from neutrophil lysates by sucrose density centrifugation, it is found that lysozyme release from neutrophils exposed to PMA or to A23187 reflects a selective disappearance of the small, peroxidase-negative (specific) granules from the cells. These studies demonstrate that neutrophils can mobilize the specific and azurophil granules independently. These studies also demonstrate that under certain conditions the specific granules of human neutrophils behave like the storage granules of secretory cells. Finally, these studies show that techniques of separating neutrophil granules according to their sedimentation characteristics successfully divide these granules into populations that are distinct not only by cytochemical and morphologic criteria but also according to their availability for mobilization and extracellular release. (APM J Pathol 87:273-284, 1977).
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PMID:The differential mobilization of human neutrophil granules. Effects of phorbol myristate acetate and ionophore A23187. 32 7

An immunocytochemical unlabelled antibody method using rabbit antihuman lysozyme, antirabbit immunoglobulin, and soluble rabbit antihorseradish peroxidase/horseradish peroxidase complexes was used to study the fine structural distribution of lysozyme in human bronchial glands. None was identified in mucous cells but there was heavy staining of the serous cell granules. The serous cell granules were not stained uniformly, suggesting the presence of other secretory products but lysozyme secretion appears to be a major function of these cells. The pathological implications of this are discussed.
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PMID:Ultrastructural immunocytochemical localisation of lysozyme in human bronchial glands. 32 82

The bactericidal action that results from lactoperoxidase-catalyzed oxidation of iodide or thiocyanate was studied, using Escherichia coli as the test organism. The susceptibility of intact cells to bactericidal action was compared with that of cells with altered cell envelopes. Exposure to ethylenediaminetetraacetic acid, to lysozyme and ethylenediaminetetraacetic acid, or to osmotic shock were used to alter the cell envelope. Bactericidal action was greatly increased when the cells were exposed to the lactoperoxidase-peroxide-iodide system at low temperatures, low cell density, or after alteration of the cell envelope. When thiocyanate was substituted for iodide, bactericidal activity was observed only at low cell density or after osmotic shock. Low temperature and low cell density lowered the rate of destruction of peroxide by the bacteria. Therefore, competition for peroxide between the bacteria and lactoperoxidase may influence the extent of bactericidal action. Alteration of the cell envelope had only a small effect on the rate of destruction of peroxide. Instead, the increased susceptibility of these altered cells suggested that bactericidal action required permeation of a reagent through the cell envelope. In addition to altering the cell envelope, these procedures partly depleted cells of oxidizable substrates and sulfhydryl components. Adding an oxidizable substrate did not decrease the susceptibility of the altered cells. On the other hand, mild reducing agents such as sulfhydryl compounds did partly reverse bactericidal action when added after exposure of cells to the peroxidase systems. These studies indicate that alteration of the metabolism, structure, or composition of bacterial cells can greatly increase their susceptibility to peroxidase bactericidal action.
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PMID:Susceptibility of Escherichia coli to bactericidal action of lactoperoxidase, peroxide, and iodide or thiocyanate. 34 97

Conjugation of lysozyme with horse radish peroxidase by means of glutaraldehyde results in a complex which retains the activities of both enzymes. The incubation of peptidoglycan with lysozyme-peroxidase followed by the reaction with 3,3'-diaminobenzidine and H2O2 results in a strong labelling of both sides. In contrast, after treatment with peroxidase alone no reaction was observed. Thus, the specific binding of lysozyme-peroxidase can be used for the electron microscopic localization of this component in the bacterial cell wall. Isolated peptidoglycane as well as trypsinized cell walls of group A and C streptococci were labelled both on the inner and the outer surface. The surface of intact cells of group A- and C-streptococci was labelled only sparsely. In contrast, by means of the indirect immunoferritin technique strong labelling of intact cells was effected with specific anti-peptidoglycan antibodies. The specificity of these antibodies are mainly directed to the peptide side chains. From this we suggest that in the cell wall of group A and C streptococci the lysozyme-sensitive part of the peptidoglycan is not so superficially localized as the peptides.
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PMID:The use of lysozyme-peroxidase-conjugates for the electron microscopic detection of peptidoglycan in the cell wall of streptococci. 35 34

An enzyme linked immunosorbent assay (ELISA) was established to detect rat serum antibodies to pneumonia virus of mice (PVM). Vero cells infected with the virus were absorbed to the surface of microplates, and the presence of antibodies in the sample evaluated were demonstrated by the subsequent use of goat anti-rat immune globulin G conjugated to peroxidase and by specific substrate. The results indicated that antibodies against pneumonia virus of mice could be detected in rat serum with the ELISA procedure. The results were reproducible, and the method was approximately eight times more sensitive than the hemagglutination inhibition procedure.
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PMID:Enzyme-linked immunosorbent assay for the detection of antibodies to pneumonia virus of mice in rat sera. 37 62

The number of white blood cells and of polymorphonuclear leukocytes remained unchanged in vervet monkeys (Cercopithecus aethiops) receiving a "O" protein diet. The motility of the polymorphonuclear leukocytes and their phagocytic and killing indices with and without leukokinin stimulation decreased in protein-depleted animals. Acid cathepsin decreased, DNA relatively increased, and peroxidase, alkaline phosphatase, acid phenylphosphatase, and lysozyme reached higher levels in the polymorphonuclear leukocytes of animals on a "O" protein diet.
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PMID:Polymorphonuclear neutrophilic leukocytes in protein deficiency. 40 70

The hairy-cells (HC) of 10 patients with hairy-cell leukaemia were studied with several techniques to evaluate their phagocytic potential. Mononuclear cells from normal donors and from patients with acute monocytic leukaemia served as controls. Light microscopically HC seemed to have ingested bacteria or latex particles. Treatment of the cells with lysostaphin, an enzyme that kills extracellular Staphylococcus aureus, showed that almost all 'ingested' bacteria were extracellular. Lanthanum nitrate, added during the fixation procedure for electron microscopy, stained both the outer cell membrane and the membranes of the 'phagosomes' of the HC, also indicating that the 'ingested' particles were extracellular. HC showed no increased oxygen consumption on exposure to bacteria in the presence of serum. Furthermore, HC showed no lysozyme or peroxidase activity, whereas non-specific esterase activity was much weaker than in monocytes. These findings, which show that HC are essentially non-phagocytic, constitute strong evidence against a monocytic origin of the malignant cells of hairy-cell leukaemia.
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PMID:Phagocytic potential of hairy cells. 49 73

Estrogen is an essential requirement for the postpubertal trophic development and maintenance of the differentiated state of the oviduct, uterus, cervix, vagina and mammary glands of mammals. Estrogen, apparently functioning through its specific cytoplasmic receptor protein via a multistep interaction pathway induces gene expression of specific biochemical events leading to growth and differentiation of target tissues (Jensen et al., Proc Natl Acad Sci, 59:632, 1968; Gorski et al., Recent Prog Horm Res 24:45, 1968). One biochemical expression of the estrogen gene is the synthesis of specific mRNA transcripts for certain specific marker proteins, including ovalbumin, lysozyme and ovomucoid in the chick oviduct (O'Malley and McGuire, Proc Natl Acad Sci 60:1527, 1968; Palmiter and Schimke, J Biol Chem 248:1502, 1973), tubulin in the mammalian oviduct (Brenner and Anderson, Handbook of Physiology 7(2):123, 1973; Brenner et al., Endocrinology 95:1094, 1974) and peroxidase (EC 1,11.1.7) in the rodent uterus (Brockelmann and Fawcett, Biol Reprod 1:59, 1969; Churg and Anderson, J Cell Biol 62:449, 1974; Anderson et al., J Cell Biol 64:668, 1975).
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PMID:Reproductive tract peroxidases as endproducts of estrogen-specific gene expression. 51 22

The absorption spectra of fluram, lysozyme, horse-radish peroxidase, and mixtures of lysozyme + fluram and peroxidase + fluram and the fluorescence and fluorescence excitation spectra of the mixtures in 0.05 M phosphate buffer with 1 per cent dioxane are determined. Due to formation of a protein-fluram compound, the absorption spectra of the mixtures are not algebraic sums of the components. From the fluorescence intensities the number of bonding sites is found 6 in both cases. The fluorescence spectrum of the peroxidase-fluram compound has maxima at 305, 350, 400, 450 nm due to peroxidase and at 480 nm originating from fluram. In mixtures of 10(-5) M lysozyme + 10(-4) M fluram, 3/4 of the excitation energy is transferred from lysozyme to fluram within the compound under 280 nm excitation. Under similar conditions 4/5 of the excitation energy is transferred from peroxidase to fluram.
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PMID:Absorption and fluorescence of fluram-labelled lysozyme and peroxidase solutions. 55 45


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