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)

The antibacterial effects of two lysozymes purified from rainbow trout kidney (type I and II) were tested on eight bacterial strains isolated from cases of clinical mastitis (staphylococci, streptococci and coliforms). Three other lytic agents were included in the experiments as controls: hen egg-white lysozyme, lysostaphin and mutanolysin. Proliferating bacteria were incubated with the various lytic agents, either in hearts infusion broth or in milk. The type II rainbow trout lysozyme decreased the number of live bacteria (colony forming units) of all the strains tested, but was most efficient against staphylococci. The other two lysozymes had little effect.
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PMID:A lysozyme isolated from rainbow trout acts on mastitis pathogens. 267 19

The lytic activity of mutanolysin from Streptomyces globisporus on 42 cultures of Actinomyces pyogenes could be effectively analyzed in an aggregometer. It was expressed as increase of transmittance at 546 nm after 20 min and 2 h at 37 degrees C. The A. pyogenes cultures revealed no uniform lysis pattern. Most of the cultures were lyzed within 20 to 40 min at 37 degrees C, others were lyzed only moderately or weakly within 2 h of incubation. The lytic activity was optimal at low (0.01 mol/l) molarity of the lysis buffer between pH 5.7 and 7 and could be inhibited by HgCl2.A. pyogenes was not lyzed by lysostaphin or lysozyme.
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PMID:Mutanolysin-induced lysis of actinomyces pyogenes determined by aggregometry. 306 68

Staphylococcal protein A, a cell wall component of several strains of Staphylococcus aureus has found many uses as a research tool, as a diagnostic reagent and even as a possible therapeutic agent in cancer. These uses have arisen exclusively out of its almost unique property of binding specifically to the Fc region of many immunoglobulin molecules. As Staphylococcus aureus is pathogenic, it has been desirable for industrial purposes to clone the gene coding for protein A into Escherichia coli and to develop a sensitive assay free from interference by bacterial components. We describe an ELISA assay which is capable of detecting staphylococcal protein A in bacterial lysates at levels as low as 1.0 ng/ml and which is free of interference from lysozyme, lysostaphin, endogenous peroxidases or other bacterial antigens.
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PMID:Development of an enzyme-linked immunosorbent assay for staphylococcal protein A produced in Escherichia coli by pUC8 based plasmids containing the Staphylococcus aureus Cowan I protein A gene. 353 92

Cells of Azotobacter vinelandii encysted in Burk's nitrogen-free liquid media which had been supplemented with n-butyl alcohol, beta-hydroxybutyrate, or crotonate. Butyraldehyde and butyrate did not influence the extent of encystment. In the absence of glucose, beta-hydroxybutyrate enhanced the rate and extent of encystment. In the presence of glucose, it promoted abortive encystment, which was manifested by the disorganization of the exine and the release of a highly viscous material into the medium. The soluble, viscous polymer was separated from the medium by a series of ethyl alcohol precipitations and identified as a mucopeptide. It was cleaved by treatment with lysozyme and lysostaphin with a concomitant increase in reducing power. It contained 13.9% N; 56% amino acids, as alanine (alanine, lysine, and glutamic acids); and 42% hexosamines. The polymer appeared to be similar to a noncross-linked peptidoglycan.
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PMID:Encystment and polymer production by Azotobacter vinelandii in the presence of beta-hydroxybutyrate. 566 5

In the present studies we compared the ability of two commonly used assays, solid-phase radioimmunoassay and enzyme-linked immunosorbent assay (ELISA), to detect human antibodies to Staphylococcus aureus peptidoglycan. ELISA was superior, with a reproducibility of 12.0%, as compared with 18.1% in solid-phase radioimmunoassay. Much lower serum dilutions could be used in ELISA. We also studied the effects of solubilizing the antigen by lysostaphin, lysozyme, or ultrasonication. Lysostaphin-treated peptidoglycan cannot be recommended since solid-phase radioimmunoassay could not distinguish positive from negative serum samples with this preparation. On the other hand, the sensitivity in both assays was high when peptidoglycan treated with lysozyme for 240 min or with ultrasonication for 30 min was used as antigen. The interassay correlation between solid-phase radioimmunoassay and ELISA was slightly better with sonicated peptidoglycan (correlation coefficient = 0.94, P less than 0.01), as compared with lysozyme-treated peptidoglycan (correlation coefficient = 0.76, P less than 0.01). We recommend the ELISA with sonicated peptidoglycan as antigen for use in routine serology.
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PMID:Methodological aspects of Staphylococcus aureus peptidoglycan serology: comparisons between solid-phase radioimmunoassay and enzyme-linked immunosorbent assay. 637 39

Staphylococcal protein A could be extracted in large amounts by simple stirring of the cells with physiological saline (pH 7.8). The amount of protein A obtained by the technique was found to be the same as obtained by lysozyme/lysostaphin techniques (45 micrograms/ml). The protein A extracted by salt-washing technique was of higher molecular weight (71,000) and differing in some biological properties like complement fixation from the protein A prepared by lysostaphin technique.
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PMID:Comparison of the bio-physical and biological properties of staphylococcal protein-A extracted by salt-washing and conventional procedure. 653 21

The experimental conditions for plasmid transfer and genetic recombination in Staphylococcus aureus and some coagulase-negative staphylococci by protoplast fusion are described. Protoplasts were prepared by treatment with lysostaphin and lysozyme in a buffered medium with 0.7 to 0.8 M sucrose. Regeneration of cell walls was accomplished on a hypertonic agar medium containing succinate and bovine serum albumin. Transfer of plasmids occurred after treatment of the protoplast mixtures with polyethylene glycol (molecular weight, 6,000) not only between strains of the same species but also between parents of different species, although at approximately 100 times lower frequency in the latter case. Recombination of the chromosomal genes in fused protoplasts required simultaneous treatment of the mixed protoplasts with polyethylene glycol and CaCl2. A method was developed for isolation of recombinants after fusion between mutants of S. areus carrying unselectable markers. Antibiotic resistance plasmids were introduced into the parental strains and used as primary markers to detect protoplast fusion. Chromosomal recombinants were found among the clones with both parental plasmids at a high frequency. The method appears to have simple applications in the construction of strains with multiple mutant characters.
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PMID:Plasmid transfer and genetic recombination by protoplast fusion in staphylococci. 700 33

The purpose of this study was to determine whether lysostaphin would enhance its anti-staphylococcal efficacy in combination with lysozyme. Minimum inhibitory concentrations (MICs) of lysostaphin and lysozyme were separately determined for 41 strains belonging to 10 different species of human staphylococci. Lysozyme was virtually inactive and showed MICs of 15 mg/ml. On the contrary, all strains were susceptible to lysostaphin and showed MICs ranging from 2.5 to 60 micrograms/ml for the different Staphylococcus species. When the MIC of lysostaphin was determined in media containing submultiples of the MIC of lysozyme, the values obtained were much lower. The reduction of the lysostaphin MIC ranged from 16- to 200-fold in the different species tested. In Staphylococcus aureus, in particular, the combination of lysostaphin with 1.5 mg of lysozyme per ml reduced the MIC of lysostaphin by 25-fold. The activities of two combinations of the two enzymes were evaluated: one combination was expected to be active on S. aureus only, and the other combination was expected to inhibit all Staphylococcus strains. The first combination (0.5 micrograms of lysostaphin plus 0.5 mg of lysozyme per ml) was inhibitory to all of the 84 S. aureus strains tested, whereas 137 of 151 strains of other Staphylococcus species were unaffected. On the contrary, all of the 235 Staphylococcus strains tested were inhibited by the second combination (4 micrograms of lysostaphin plus 5 mg of lysozyme per ml). The possible mechanisms of lysostaphin potentiation by lysozyme are considered, and the potential use of a lysostaphin-lysozyme combination for topical therapy of staphylococcal infections resistant to other antibiotics is discussed.
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PMID:High-level potentiation of lysostaphin anti-staphylococcal activity by lysozyme. 708 76

A total of 57 gram-positive, catalase-positive cocci, considered etiological agents of clinical and subclinical bovine mastitis, were tested for glucose and mannitol fermentation, coagulase and thermonuclease production, sensitivity to lysostaphin, gelatin hydrolysis, lysozyme, phosphatase and egg yolk factor production, hemolytic properties, antibiotic sensitivity, susceptibility to human and bovine phages, and enterotoxin production. All 57 strains were identified as staphylococci. A good correlation was found between 3+ and 4+ coagulase reactions, thermonuclease production, and high sensitivity to lysostaphin. Neither mannitol fermentation nor production of other enzymes appeared to be a specific property of bovine Staphylococcus aureus strains. beta- and delta-hemolysins were more frequently found than alpha-hemolysin. Nearly 40% of the strains were penicillin resistant. Strains were lysed by phage 42E from the human phage set more frequently than by phage 42D, whereas with the bovine set, strains were more sensitive to specific bovine phages. Three strains produced enterotoxin C, and one strain produced enterotoxin D.
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PMID:Characterization of staphylococci isolated from mastitic cows in Spain. 738 55

The capsular polysaccharide released from the bacterial surface by cell wall turnover during growth exhibited less size heterogeneity and a higher average molecular mass than the polysaccharide extracted from the cell by treatment with lysostaphin or low pH. Treatment of turnover polysaccharide, radiolabelled by growth of the bacteria in the presence of N-acetyl-[3H]-glucosamine, with muramidase B from Chalaropsis released a low molecular weight product chromatographically identical to the peptidoglycan degradation products released from the peptidoglycan-teichoic acid complex by the same treatment. It is concluded that some or all of the capsular polysaccharide released into the culture fluid during growth is derived from peptidoglycan-linked capsular material, solubilised by cell wall turnover.
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PMID:The capsular turnover product of Staphylococcus aureus strain Smith. 801 80


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