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)

Patients who had received long-term therapy with practolol and other beta-adrenergic receptor blocking drugs were examined ophthalmologically. Tear lysozyme concentration and serum autoantibodies (antinuclear antibodies, DNA-binding antibodies and intercellular cement substance antibodies) were measured. It was found that beta-adrenergic receptor blocking drugs may have a pharmacological effect on the lachrymal glands, but this was not associated with dry eyes or adverse reaction. Practolol was found to be capable of reducing tear lysozyme concentrations to very low levels, and this was initially associated with high titres of ICC antibody. No other drug tested produced these effects.
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PMID:Beta-adrenergic receptor blocking drugs: tear lysozyme and immunological screening for adverse reaction. 1 31

Sedimentation method has been used to study hen egg-white lysozyme binding to glucosylated (from T2 phage) and non-glucosylated (from calf thymus) DNA under conditions similar to physiological ones (pH 7,3--7,4, ionic strength 0.07--0.24). The results indicate that lysozyme binds cooperatively to both DNA's. Binding parameters have been obtained by applying the theory of one-dimensional adsorption of small molecules on a linear homopolymer. X-ray patterns of complexes with different protein content have been obtained.
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PMID:[DNA complexes with lysozyme]. 3 32

Actinomyces viscosus homogenate (AVIS) contins substance(s) which cause spleen cells from conventional and germfree mice to undergo increased DNA synthesis. This mitogenic effect is primarily on B cells since spleen cells from nude mice or T-depleted spleen cells from conventional mice respond as strongly as conventional (T + B) spleen cells. Mouse thymocytes do not respond mitogenically to AVIS. It is unlikely that the mitogenic acitivity is due to the presence of LPS, since A. viscosus is Gram-positive and is not known to have an LPS cell wall component. Also, AVIS is not inactivated by polymyxin B, as are some preparations of LPS, and C3H/HeJ mouse splenocytes respond strongly to AVIS but not to LPS. The activity is heat stable, is not lost upon dialysis, and is not affected by lysozyme. Mitogenic activity is partially lost when AVIS is digested with nonspecific bacterial protease or treated with metaperiodate. Sodium hydroxide treatment completely abolishes mitogenic activity. Actinomycotic lesions are characterized by a long-tern inflammatory response involving a dense plasma cell infiltrate. We suggest that B cell mitogens form Actinomyces may play a role in the elicitation of the plasma cell component of these lesions.
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PMID:Mitogenic activity of Actinomyces viscosus. I. Effects on murine B and T lymphocytes, and partial characterization. 6 95

Sequential reverse transcriptase, DNA polymerase, and S1 nuclease reactions can be employed to synthesize double-stranded DNA representing messenger RNA. Using reverse transcriptase products made from partially purified lysozyme, ovomucoid, and ovalbumin messengers from hen oviduct, we have characterized the Escherichia coli DNA polymerase I reaction. We have optimized for a high yield of full length second strands under conditions which require only a small amount of mRNA. The effects of several parameters (time, enzyme levels, salt concentration, monovalent cation, and temperature) on the length of products synthesized by DNA polymerase I have been investigated. Each has a significant influence on the proportion of products which are full length. Under our conditions the three reactions are efficient in synthesizing full length duplex DNA from partially purified mRNA fractions or from total poly(A)-containing RNA.
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PMID:Synthesis of double-stranded DNA complementary to lysozyme, ovomucoid, and ovalbumin mRNAs. Optimization for full length second strand synthesis by Escherichia coli DNA polymerase I. 7 87

Thymus cells from mice primed s.c. with a high dose (10 mg) of lysozyme (Lys) specifically suppressed delayed footpad reaction (FPR) in mice previously immuned with lipid-conjugated lysozyme (D.Lys), and also suppressed the transfer of FPR by D.Lys-immune spleen cells into normal mice. Furthermore, they inhibited antigen-stimulated DNA synthesis of D.Lys-immune spleen cells in vitro. If the suppressor thymus cells were cultured with Lys in vitro, they produced soluble factor which depressed the ability of D.Lys-immune spleen cells to transfer FPR. Both supernatant of culture without Lys and extract of suppressor thymus cells were inactive in supression of FPR. The suppressor factor was antigen-specific because its suppressive activity was absorbed with Lys but not with an unrelated antigen lactalbumin. The factor failed to depress the ability of D.Lys-immune spleen cells to transfer FPR when the spleen cells were depleted of glass-adherent cells. In addition, incubation of peritoneal exudate cells from normal mice with the factor rendered the cells suppressive for passive transfer of FPR. These results suggest that the suppressor factor depresses the effector function of T cells responsible for FPR possibly via macrophage.
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PMID:Regulatory role of suppressor T cells in the expression of delayed-type hypersensitivity in mice. II. Soluble factor from thymic suppressor cells stimulated with antigen in vitro and its possible interaction with macrophages. 9 73

Normal sera and plasma, derived from humans, calves, rats, rabbits, horses, human synovial fluids, inflammatory exudates, and leukocyte extracts, when sufficiently diluted are highly bacteriolytic for Staph, aureus, Strep. faecalis, B. sutilis and to a variety of gram-negative rods. On the other hand, concentrated serum or the other body fluids are usually not bacteriolytic for these bacterial species. While the lysis of Staph, aureus and B. subtilis by diluted serum is not lysozyme dependent, lysis of Strep. faecalis is absolutely dependent on the concentration of lysozyme. The lytic factor in human serum is present in Cohn's fractions III, IV, and V. It is nondialyzable, resistant to heating for 75 degrees C and 20 min, and acts optimally at pH 5.0. Like leukocyte extracts, synovial fluids, and inflammatory exudates, it lyses only young staphylococci. The inability of concentrated serum to lyse Staph. aureus and Strep. faecalis is due to the presence in the gamma globulin fraction of a potent inhibitor, which can be partly removed by dilution of by adsorption upon the homologous bacteria. Lysis of the bacteria is also strongly inhibited by Cohn's fraction II (gamma globulin) by high-molecular-weight DNA, heparin, liquoid, and histone. The possible role played by serum globulin in the protection of bacteria against degradation by leukocyte is discussed.
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PMID:Effect of leukocyte hydrolases on bacteria. XIV. Bacteriolytic effects of human sera, synovial fluids, and purulent exudates on Staphylococcus aureus and Streptococcus faecalis: modulation by Cohn's fraction II and by polyelectrolytes. 9 58

Leukocyte extracts, trypsin, and lysozyme are all capable of releasing the bulk of the LPS from S. typhi, S. typhimurium, and E. coli. Bacteria which have been killed by heat, ultraviolet irradiation, or by a variety of metabolic inhibitors and antibiotics which affect protein, DNA, RNA, and cell wall synthesis no longer yield soluble LPS following treatment with the releasing agents. On the other hand, bacteria which are resistant to certain of the antibiotics yield nearly the full amount of soluble LPS following treatment, suggesting that certain heatlabile endogenous metabolic pathways collaborate with the releasing agents in the release of LPS from the bacteria. It is suggested that some of the beneficial effects of antibiotics on infections with gram-negative bacteria may be the prevention of massive release of endotoxin by leukocyte enzymes in inflammatory sites.
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PMID:Effect of leukocyte hydrolases on bacteria. XV. Inhibition by antibiotics, metabolic inhibitors, and ultraviolet irradiation of the release by leukocyte extracts, trypsin, and lysozyme of lipopolysaccharide from gram-negative bacteria. 9 59

Under experimental conditions of genetic transformation, protamine and total histone were bactericidal for Bacillus subtilis cells. The abilities to cause lethality were very similar for both, either protamine or histone, with no antagonistic effects amongst these natural polycations. With both basic proteins acting simultaneously the enhancement was higher than a summation of the separate lethal effects. Sublethal concentration of protamine added at the beginning of transformation time, produced a strong inhibition of transforming efficiency. The same concentration added later than 10 min from the start of transformation had no inhibitory effect. These facts together with the absence of inhibition by simple pretreatment of DNA alone as well as the cell protection by protamine against lytic activity of lysozyme, suggest a protamine-cell surface interaction which impedes DNA uptake events.
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PMID:Lethal effect of protamine and histone on competent Bacillus subtilis cells. Inhibition of genetic transformation by protamine in sublethal concentration. 11 Oct 2

A simple preparative method is described for isolation of the cytoplasmic and outer membranes from E. coli. The characteristics of both membrane fractions were studied chemically, biologically, and morphologically. Spheroplasts of E. coli K-12 strain W3092, prepared by treating cells with EDTA-lysozyme [EC 3.2.1.17], were disrupted in a French press. The crude membrane fraction was washed with 3 mM EDTA-10% (w/v) sucrose, pH 7.2, and the cytoplasmic membranes and outer membranes were separated by sucrose isopycnic density gradient centrifugation. The crude membrane fraction contained approximately 10% of the protein of the whole cells, 0.3% of the DNA, 0.7% of the RNA, 0.3% of the peptidoglycan, and about 30% of the lipopolysaccharide. The cytoplasmic membrane fraction was rich in phospholipid, while the outer membrane fraction contained much lipopolysaccharide and carbohydrate; the relative contents of lipopolysaccharide and carbohydrate per mg protein in the cytoplasmic membrane fraction were 12 and 40%, respectively, of the contents in the outer membrane fraction. Cytochrome b1, NADH oxidase, D-lactate dehydrogenase [EC 1.1.1.28], succinate dehydrogenase [EC 1.3.99.1], ATPase [EC 3.5.1.3], and activity for concentrative uptake of proline were found to be localized mainly in the cytoplasmic membranes; their specific activities in the outer membrane fraction were 1.5 to 3% of those in the cytoplasmic membrane fraction. In contrast, a phospholipase A appeared to be localized mainly in the outer membranes and its specific activity in the cytoplasmic membrane fraction was only 5% of that in the outer membrane fraction. The cytoplasmic and outer membrane fractions both appeared homogeneous in size and shape and show vesicular structures by electron microscopy. The advantages of this method for large scale preparation of the cytoplasmic and outer membrane fractions are discussed.
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PMID:Cytoplasmic membrane vesicles of Escherichia coli. A simple method for preparing the cytoplasmic and outer membranes. 12 74

Effect of alkaline earth metal ions on induction of the competence for DNA transfection was investigated. Unlike spheroplasts, the bulk of the bacteria treated with these ions retains colony-forming ability. The order of effectiveness for transfection of phiA replicative-form DNA has been found to be Ba2+ greater than Ca2+ greater than Sr2+ greater than Mg2+. The competence of Ba2+-treated cells is 3 to 5 times higher that that of Ca2+-treated bacteria and about 40 times higher than that of lysozyme-EDTA spheroplasts. The Ba2+-dependent transfection is cryophilic and formation of the infective complex occurs very rapidly at 0 degrees C, But not at 37 degrees C.
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PMID:Sensitivity of Escherichia coli to viral nucleic acid, X. Ba2+-induced competence for transfecting DNA. 12 94


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