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)

Lysozyme (LZM) concentrations in synovial fluid were determined in patients with seropositive and seronegative rheumatoid arthritis (RA) and in patients whose arthritic exudates had been caused by Reiter's disease, a Yersinia enterocolitica infection, osteoarthritis, or trauma. Patients with rheumatoid disease had significantly higher levels of lysozyme in synovial fluid than patients with non-rheumatic diseases. The concentration of lysozyme correlated with the number of polymorphonuclear leukocytes in synovial fluid in seronegative--but not in seropositive--rheumatoid arthritis. In patients with rheumatic arthritis the lysozyme level correlated inversely with the concentration of glucose in synovial fluid. In patients with rheumatoid pleural effusion, lysozyme levels in pleural fluid were comparable to those in serum. The concentration of LZM in thoracic duct lymph was roughly the same as in serum. During drainage of thoracic duct lymph, the lysozyme level in serum decreased.
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PMID:Lysozyme concentrations in synovial fluid, pleural fluid and thoracic duct lymph in rheumatoid arthritis. 400 80

Muzolimine, the new sulphonamide-free loop-diuretic with both high ceiling and long-lasting activities, was tested in 21 adult patients with chronic renal failure (CRF) (creatinine clearance ranging from 30 to 5 ml/min) and acute fluid overload. Low-protein diet and individual drug therapy were unchanged throughout the study. All patients received a single oral dose of 240 mg of muzolimine for 4 or 6 consecutive days depending on individual response. Clinical status, diuresis, body weight, blood and urine chemistry were recorded daily. In 19 out of 21 patients muzolimine treatment induced reversal of edema and congestive heart failure and a satisfactory fluid balance was achieved. Only two patients did not respond to diuretic treatment and required dialysis to control fluid balance and azotemia. In responsive patients diuresis increased by 50-100% and no rebound antidiuresis was observed after drug withdrawal. Body weight decreased meanly by 9%. No significant change occurred in serum concentration of K throughout the study, even in the 11 patients on digoxin. Except for a slight decrease of serum Cl by the end of treatment, no significant change in serum electrolytes was recorded. No effect was observed on blood glucose, urea and creatinine clearance whereas a slight increase of serum uric acid was recorded. Urinary lysozyme and gamma-GT were similar before and after the trial. Apart from a single case of muscle cramps, no significant side-effects were recorded. In conclusion, the present results indicate that short-term, high-dose oral muzolimine treatment is effective and safe in most patients with advanced CRF and acute fluid retention.
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PMID:Short-term, high-dose muzolimine treatment in patients with chronic renal failure and acute fluid retention. 400 85

Pep 5 and nisin are cationic bactericidal peptides which were shown to induce autolysis in Staphylococcus cohnii 22. In contrast to nisin, Pep 5 induced lysis could be stimulated in the presence of glucose. Addition of lipoteichoic acids (LTA) (D-alanine:phosphorus = 0.475:1) inhibited all effects of Pep 5 on susceptible cells in a molar ratio LTA:Pep 5 of 10:1. Treatment of S. cohnii 22 with Pep 5 or nisin for 20 min and subsequent washing with 2.5 M NaCl released autolysin activity. Crude preparations of the hydrolyzing enzymes produced free amino groups as well as polysaccharide fragments from the murein backbone, suggesting the presence of a muramidase or glucosamidase, and endopeptidase or amidase. Both enzyme activities were inhibited by lipoteichoic acid; they could be fully reactivated by addition of Pep 5 in sufficient concentrations. The velocity of hydrolysis was not influenced by nisin, whereas it was doubled in presence of Pep 5. The results are discussed in view of a possible mechanism of induction of lysis by Pep 5 and nisin.
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PMID:Induction of autolysis of staphylococci by the basic peptide antibiotics Pep 5 and nisin and their influence on the activity of autolytic enzymes. 400 48

The structure of polysaccharide prepared by lysozyme digestion from the cell wall of Propionibacterium acnes strain C7 was examined. The polysaccharide fraction was composed of glucose, galactose, mannose, galactosamine, and diaminomannuronic acid in a molar ratio of 1:1:0.3:1:2. By Smith degradation of the polysaccharide, diaminouronic acid-containing fractions were obtained, and the configuration of diaminouronic acid was identified as 2,3-diacetamido-2,3-dideoxymannuronic acid [Man(NAc)2A] by means of 1H-NMR and 13C-NMR spectroscopic analyses. The results of analyses involving methylation and partial acid hydrolysis led to the conclusion that the polysaccharide has the repeating unit----6)Gal(alpha 1----4)Man(NAc)2A(beta 1----6)Glc(alpha 1----4)Man(NAc)2A (beta 1----3)GalNAc(beta 1--. In addition, a portion of the galactose residues were substituted at C-4 by alpha 1----2 linked mannotriose.
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PMID:Structure of acidic polysaccharide from cell wall of Propionibacterium acnes strain C7. 403 Jul 44

Increased production of sinefungin, a very potent antifungal and antiparasitic nucleoside antibiotic was achieved by medium and strain improvement. When soybean-meal, dextrin and yeast extract were added as carbon and nitrogen sources to the fermentation medium, instead of corn steep liquor, soya-oil and glucose; the antibiotic yield increased from 40 micrograms/ml to 126 micrograms/ml with low biomass production. Strain improvement was attempted by two methods. The mean antibiotic yield of the variants after multistep mutagenesis by N-methyl-N'-nitro-N-nitrosoguanidine and ethyleneimine was 466 micrograms/ml. Protoplasts of the parental strain were prepared by lysozyme digestion from mycelia grown in a medium containing 0.7% glycine. The mean activity of the regenerated protoplasts was 664 micrograms/ml. Thus, the overall sinefungin production could be increased 16-fold.
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PMID:Enhanced sinefungin production by medium improvement, mutagenesis and protoplast regeneration of Streptomyces incarnatus NRRL 8089. 406 2

A method has been developed for the isolation of outer membranes from Acinetobacter sp. strain MJT/F5/199A. Washed cells were broken in a French press and, after deoxyribonuclease and ribonuclease treatment, removal of intact cells, and four washes in 20 mosmol phosphate buffer, pH 7.4, with centrifugation at 25,000 x g for 10 min, preparations of cell wall fragments from which almost all pieces of plasma membrane had been removed resulted. Treatment of the cell walls with lysozyme and further washing, in the presence of 20 mM MgCl(2), yielded preparations of outer membranes. Electron microscopy of freeze-etched preparations shows that a regular pattern of subunits is present on the outer surfaces of intact cells. After negative staining, these subunits are visible on isolated walls and outer membranes; they can be removed by brief treatment with papain. In section, the cell wall structure is that typical of gram-negative bacteria, but the subunits are not detectable on the surface of the outer membrane. The outer membrane retains the appearance of a "unit membrane" in the cell wall, isolated outer membrane, and papain-treated outer membrane fractions. Both cell walls and outer membranes contain a high percentage of protein (76 and 84%, respectively) and not more than 5% carbohydrate, of which glucose and galactose are constitutents. The outer membranes of this Acinetobacter thus differ in structure and composition from those of bacteria in the Enterobacteriaceae.
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PMID:Isolation of outer membranes with an ordered array of surface subunits from Acinetobacter. 412 37

The Streptococcus mutans group b antigen of strain FA1 has been defined as to chemical composition and immunological specificity. The antigen in cold trichloroacetic acid extracts was fractionated on diethylaminoethyl-Sephadex A-25 at pH 8.5. Two forms were isolated: a polysaccharide and a mucoprotein. The two polymers reacted as a single substance in agar gel diffusion against specific adsorbed FA1 rabbit antisera but were separated by gel immunoelectrophoresis. No reaction with any other S. mutans or streptococcal group sera occurred. Galactose composed about one-third and galactosamine about 3% of the total weight of each polymer. Rhamnose was a major component of the polysaccharide (47%) but was present only in traces in the mucoprotein. The protein content of the latter was about 40%. No significant quantities of glycerol, phosphorus, or muramic acid were present in either case. Pepsin and trypsin had no effect on the serological specificity of the mucoprotein. d-Galactose and d-galactosamine were strong inhibitors (70%) of the precipitin reaction, whereas d-glucose, d-glucosamine, and N-acetyl-d-glucosamine inhibited between 25 and 35%. The results indicate that the antigen is a major antigenic component of the cell wall and that the specificity of the antigen resides in binding sites which contain both d-galactose and d-galactosamine. Agglutination of whole cells by specific group b antiserum indicates the antibody receptor sites of the polysaccharide antigen are at the surface of the streptococcal cell. The mucoprotein, but not the polysaccharide, was released from the cell by lysozyme. Lysis did not occur. The immunological specificity and other characteristics of the antigen establishes it as the identifying antigen of S. mutans group b.
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PMID:Structure and immunological specificity of the Streptococcus mutans group b cell wall antigen. 412 3

The peroxidase of human parotid saliva has been purified by concentration, gel filtration on Sephadex G-200, and ion exchange chromatography on Amberlite CG-50. The purified product was devoid of amylase activity, lysozyme activity, and immunoglobulin A (IgA). However, it had an inhibitory effect on the growth of Lactobacillus acidophilus in complete growth medium and on lysine accumulation by L. acidophilus in a buffer-glucose medium, when combined with thiocyanate ions. The concentrations of peroxidase and thiocyanate ions employed were within the range found in saliva. The fractions which contained IgA did not have an anti-bacterial effect on L. acidophilus under the conditions employed. Parotid saliva also contained low molecular weight inhibitors of peroxidase activity. These studies support the involvement of the salivary peroxidase in an antibacterial system in saliva.
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PMID:Antibacterial activity of the purified peroxidase from human parotid saliva. 418 66

An antigen of Streptococcus mutans has been extracted from HS6 (group "a") whole cells and repeatedly fractionated by Sephadex chromatography. The antigen is shown to be a polysaccharide and contains the S. mutans group "a" antigenic site and also a second antigenic site which is common to "a" strains and 2 of 3 group "d" strains. Immunological electrophoretic and chromatographic data indicate that the two sites exist in a single molecule. The polysaccharide has a molecular weight of 107,000 and is composed of glucose, galactose, glucosamine, and galactosamine. No significant quantities of lipid, phosphorus, glycerol, or ribitol are present. Immunological specificity of the group "a" polysaccharide site depends primarily on a d-glucose . d-glucose sequence, the "a-d" site on a terminal d-galactose. Water at 100 C and pepsin (pH 2.5) at room temperature are very effective in extracting the polysaccharide from lyophilized S. mutans cells. Trypsin and lysozyme are less effective. The antigen-antibody combining site appears to be located at the cell wall surface. A small quantity of enzyme-resistant protein (5%) is firmly linked to the antigen and is considered to be a remnant of a protein to which the polysaccharide is attached in the cell wall. The composition of the protein does not identify it as a part of the peptidoglycan. No reaction to the purified polysaccharide is obtained with antisera specific for teichoic acid glycerophosphate polymers from streptococci, staphylococci, or lactobacilli.
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PMID:Extraction, purification, and chemical and immunological properties of the Streptococcus mutans group "a" polysaccharide cell wall antigen. 419 54

A mutant of Escherichia coli has been found to have an increased sensitivity to actinomycin D and to sodium deoxycholate and an unusual morphology which accompanies an abnormality in cellular division. All of these characteristics are suppressed when the strain is grown in the presence of d-alanine. This strain, called MAD-1, for murein altered division mutant, exhibits its pleiotropic phenotype only when certain carbon compounds are used as energy sources in minimal medium. Nonpermissive carbon sources, which elicit the disturbed phenotype, include glucose, mannitol, fructose, maltose, and lactose; permissive carbon sources include galactose, glycerol, lactate, and succinate. The mutant is able to transport nonpermissive carbon compounds; 3 mM 3',5'-cyclic adenosine monophosphate included in the medium does not alter the phenotype seen with growth on glucose. Deoxyribonucleic acid and protein synthesis are normal with respect to cellular mass increase. d-Alanine specifically suppresses the pleiotropic phenotype at a concentration six times lower than l-alanine, the only other compound found to be effective. There is no abnormality in the K(m) or V(max) of l-alanine racemase or d-alanine-d-alanine synthetase of MAD-1 compared to its parent, CR34. MAD-1 is more susceptible to growth inhibition by penicillin or cycloserine than its parent, and is exquisitely sensitive to lysis in the presence of sodium deoxycholate or lysozyme. When cell wall biosynthesis is inhibited, MAD-1 lyses much more rapidly than CR34, even after it has been phenotypically suppressed by growth on d-alanine. The incorporation of l-alanine and diaminopimelic acid into the peptidoglycan of the mutant and wild type is identical; d-alanine is incorporated 1.5 times more rapidly into MAD-1 cells grown under nonpermissive conditions. The peptidoglycan fragments seen after digestion with lysozyme were similar for MAD-1 and the wild type. The results are interpreted as being compatible with an increased autolytic rate in MAD-1, caused either by an increase in the quantity or activity of an autolysin, or by an abnormal cell wall which is especially susceptible to autolysis, but which was not detected by analysis of peptidoglycan fragments.
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PMID:Relationship between permeability, cell division, and murein metabolism in a mutant of Escherichia coli. 426 3


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