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)

On treating the blue green alga Anacystis nidulans with dimethylsuberimidate up to 70% of the free NH2 of the photosynthetic membrane is amidinated, and presumably inter- and intramolecular cross-links are established in the membrane proteins. Amidination destroys the ability of A. nidulans to photoreduce HCO3(-) but leaves the photochemical activities of Photosystems II and I nearly intact. With added electron acceptors, photosynthetic O2 evolution can be demonstrated both with permeable cells (permeaplasts) prepared by digestion of the cell wall of dimethylsuberimidate-reacted A. nidulans with lysozyme, as well as with heavy membrane particles (36 000 x g) prepared from dimethylsuberimidate-reacted cells. Permeaplasts prepared from dimethylsuberimidate-reacted cells resist damage in hypoosmotic medium, whereas those prepared from unreacted cells are induced to release C-phycocyanin. On the other hand, the former are inactivated more easily by heat stress than the latter. On this basis, it is concluded that cross-linking with dimethylsuberimidate confers functional instability to photosynthetic membranes.
Biochim Biophys Acta 1977 Sep 14
PMID:Photosynthetic activity of diimidoester-modified cells, permeaplasts, and cell-free membrane fragments of the blue-green alga Anacystis nidulans. 40 32

Phagocytosis and degradation of cell walls by peritoneal macrophages obtained from Fischer 344 or Buffalo rats was measured in tissue culture. Group A cell wall antigen, detected by immunofluorescence, persisted in cultured rat macrophages for at least 40 days, whereas group D cell wall material was eliminated by 6 to 8 days. This same pattern of persistence of group A cell walls and elimination of group D cell walls was observed in cultures of human monocytes followed for 24 days in culture. Group A streptococcal cell walls labeled with either [14C]alanine or [14C]glucose were handled in a similar manner by macrophages from either Fischer 344 or Buffalo rats. In contrast, [14C]glucose-labeled group D cell walls were degraded at a much faster rate. Buffalo macrophages were more efficient than Fischer 344 macrophages in degrading group D cell walls. The inability of macrophages to degrade group A cell walls was not due to a failure of lysosomes to fuse with phagosomes. Neither serum lysozyme in the culture medium nor cell wall-associated autolysin contributed to the degradation of group D cell walls by macrophages. Neither immune serum nor macrophages obtained from specifically immunized rats influenced phagocytosis or persistence of group A cell walls.
Infect Immun 1977 Sep
PMID:Processing of streptococcal cell walls by rat macrophages and human monocytes in vitro. 40 78

Thin sections of the cell wall of Sporosarcina ureae revealed two structurally distinct layers: a continuous amorphous zone, approximately 15 nm thick, which was adjacent to the plasma membrane, and an overlying periodic zone, approximately 16 nm thick. Sequential Triton X-100 and lysozyme treatment of isolated walls produced small fragments of the outer regular structure which allowed high-resolution, negatively stained images suitable for optical diffractometric analysis. These data suggested a tetragonal array of complex polygonal units of C-C spacing = 12 nm, with each unit joined to another by two delicate linkers. The array was entirely proteinaceous, consisting of a 150,000-dalton polypeptide which had a high affinity for Mg2+. It proved to be sensitive to chelating agents, 5 mM concentrations of Ca2+, Sr2+, or Ba2+, proteases, heat greater than or equal to 45 degrees C, sodium dodecyl sulfate, and pH greater than or equal to 5.8, but magnesium offered protection against the chelating agents and the deleterious salts.
J Bacteriol 1979 Sep
PMID:Surface arrays on the wall of Sporosarcina ureae. 47 3

The purified lysozyme excreted by Staphylococcus aureus strains promotes elongation and spreading on plastic surfaces and stimulates DNA synthesis of human fibroblasts (WI38). This enzyme also raises twofold the saturation density level of cultures of these cells. It is suggested that the primitive and main effect of lysozyme on fibroblasts is the triggering of morphogenesis.
Cell Biol Int Rep 1979 Sep
PMID:Effects of Staphylococcus aureus lysozyme on human fibroblasts. 49 87

Dogs were given gentamicin (10 mg/kg) intramuscularly every 8 hr for 10 days. Levels of serum creatinine rose by day 6 (0.91 +/- 0.08 vs. 0.75 +/- 0.02 mg/dl for controls, P less than 0.05) and of blood urea nitrogen by day 8 (24.3 +/- 4.80 vs. 16.1 +/- 0.90 mg/dl for controls, P less than 0.05). Gentamicin nephrotoxicity occurred earlier and was more marked when furosemide (2 mg/kg) was added: the level of serum creatinine by day 6 was 1.62 +/- 0.25 mg/dl (P less than 0.05), and the level of blood urea nitrogen by day 8 was 181 +/- 23.5 mg/dl (P less than 0.01). Elevations in the activities of the urinary enzymes beta-glucuronidase, N-acetyl-beta-glucosaminidase, and muramidase preceded rises in levels of serum creatinine and blood urea nitrogen. Examination of serial percutaneous renal biopsy specimens showed that gentamicin administration was associated with hyaline droplet degeneration, lysosomal changes, and, later, cell necrosis (primarily of the proximal tubules). Changes in renal morphology were more severe and occurred earlier when furosemide was administered concomitantly. In summary, furosemide enhanced gentamicin nephrotoxicity. Enzymuria was an early sign of gentamicin nephrotoxicity.
J Infect Dis 1979 Sep
PMID:Furosemide enhancement of experimental gentamicin nephrotoxicity: comparison of functional and morphological changes with activities of urinary enzymes. 50 Nov 48

1. Some mucus glycoproteins form soluble complexes with lysozyme at neutral pH values. 2. The extent of complex-formation was determined, by an ultracentrifugal difference method, for a range of glycoproteins covering the common blood-group specificities. 3. Interaction was strongest with those glycoproteins of blood-group Lea specificity; these were also richest in sialic acid. 4. Interaction diminished with increase of ionic strength, and was not detectable at I 0.50; however, an asialoglycoprotein was found to retain some activity. The interaction is accordingly primarily, but probably not exclusively, coulombic in origin. 5. The buoyant density of lysozyme in CsCl, CsBr, CsI and Cs2SO4 was determined; the values in the last three salts are anomalously high. This finding accounts for the previously noted difficulty of separating free protein from glycoproteins by single-stage centrifugation in CsBr. 6. Conditions for effective separation of glycoproteins from secretions containing lysozyme by density-gradient centrifugation are reported.
Biochem J 1979 Sep 01
PMID:An interaction between lysozyme and mucus glycoproteins. Implications for density-gradient separations. 51 51

The effects of dextran on renal ultrastructure and on the handling of protein by renal proximal tubules were evaluated in dextran-tolerant rats. In vivo and in vitro systems were studied by a combination of electron microscope and cell fractionation techniques. Dextran was demonstrated by electron microscopy in endocytic vacuoles and lysosomes ing a dextran-retaining fixative, and there was an increase in the number and size of the lysosomes in the proximal tubule cells using a dextran-retaining fixative, and there was an increase in the number and size of the lysosomes in dextran-treated rats. A lysosomal accumulation of dextran was also demonstrated when 3H-dextran T-80 was injected i.v. and the renal cortex analyzed by tissue fractionation. When radioactive lysozyme was injected into dextran-treated rats, there was less filtration of the protein in the kidneys than there was in the controls, but the rate of degradation of the labeled protein in slices prepared from the renal cortex and incubated in vitro was the same in the two groups. Electron microscope autoradiography revealed that radioactive lysozyme reabsorbed by the tubule cells had a similar location in both control- and dextran-treated rats. It is concluded that lysosomal protein catabolism is not altered by the presence of dextran despite pronounced ultrastructural changes in the lysosomal system. The decreased filtration of labeled protein after dextran infusion is probably related to the decreased GFR during and immediately after the dextran infusion.
Kidney Int 1979 Sep
PMID:Effects of dextran on lysosomal ultrastructure and protein digestion in renal proximal tubule. 52 77

The results of the study of the effect of various concentrations of egg lysozyme on M. luteus and M. varians using 2 methods, i.e. serial dilutions in agar and turbidimetric are presented. It was found that the MIC of lysozyme for M. luteus ranged within wide limits, from less than 0.0003 to 1 mg/ml. M. varians was stable to lysozyme. The MIC for all the strains was 8 mg/ml. The turbidimetric method provided determination of general regularities in changes of the optical density in all the strains of M. luteus under the effect of various concentrations of lysozyme. On the basis of these data it was possible to consider the method as the most deep means for determining the intraspecies similarities in the surface structures of Micrococcus as compared to the method of serial dilutions in agar. The dynamics of the changes in the optical density of the M. luteus suspension markedly differed from that of M. varians.
Antibiotiki 1978 Sep
PMID:[Action of egg lysozyme on representatives of the family Micrococcaceae. Its action on Micrococcus]. 56 55

Double-stranded chicken lysozyme cDNA was synthesized from an oviduct mRNA fraction enriched for lysozyme mRNA. The ds-cDNA was inserted into the BamHI site of plasmid pBR322 using chemically synthesized DNA linker molecules containing the BamHI restriction endonuclease cleavage site. After bacterial transformation, colonies carrying lysozyme DNA were identified by hybridization with highly purified lysozyme cDNA. The 555 base pairs long cloned DNA fragment of one recombinant plasmid was isolated and characterized by restriction endonuclease digestion. The DNA sequence of selected parts of the inserted DNA is as predicted from the amino acid sequence of prelysozyme. The sequence data allows the unambiguous location of the coding region within lysozyme mRNA.
Nucleic Acids Res 1978 Sep
PMID:Cloning of chicken lysozyme structural gene sequences synthesized in vitro. 56 56

The effect of gentamicin sulphate and its combination will prodigiozan on antibody formation in experiments and the levels of the immunobiologic reactivity of patients with purulent inflammatory processes was studied with a purpose of developing rational schemes of antibiotic therapy of infectious diseases. A decrease in the titers of the antibodies to Aeromonas and the number of antibody-forming cells in the spleen was noted on repeated administration of gentamicin to albino mice in a dose of 20 mg/kg. This was prevented by the use of prodigiozan in a dose of 500 micrograms/kg once every 4 days. The use of gentamicin in patients with purulent inflammatory diseases in doses of 40 or 80 mg twice a day for 7--10 days had no significant effect on the titers of IgA, IgG, IgM, lysozyme blood serum levels, serum bactericidal activity and absorption activity of the peripheral blood neutrophils. Still, it induced a marked suppression of the neutrophil digestive capacity as compared to the initial levels, especially on administration of gentamicin in a dose of 40 mg twice a day. An increase in the level of IgM and no suppression of the neutrophil digestive capacity were noted after completion of the therapy in the patients treated with gentamicin administered in a dose of 40 mg twice a day and prodigiozan administered in a dose of 50 micrograms once every 4 days. It is recommended to use prodigiozan in combinaed therapy with gentamicin for correction of the changes in the specific and nonspecific protective forces of the host.
Antibiotiki 1979 Sep
PMID:[Effect of gentamycin in combination with prodigiozan on the immunological reactivity of the body]. 57 85


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