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

---

Query: EC:3.2.1.17 (lysozyme)
21,489 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Protective activity of an acidic fraction of bakers' yeast mannan containing protein and phosphorus, designated as WAM025, against infection of Staphylococcus aureus beta H 248 strain in mice was investigated. WAM025 elicited a marked increase in the survival ratio of mice challenged with viable cells of the S. aureus strain, 5 X 10(8) cells per mouse, when the fraction was administered to mice 150 mg/kg/d, 5 times, intraperitoneally. This effect was stronger than that of WNM, a neutral fraction of mannan obtained from the same bakers' yeast. The difference seemed to correlate with the strength of activating effects of WAM025 and WNM on the reticuloendotherial system of the host animal. WAM025 induced higher activities of serum lysozyme and carbon clearance in mice than WNM. Also, mice treated with WAM025 showed a greater increase in number and activity of oxygen-generating blood polymorphonuclear leucocytes than mice treated with WNM.
...
PMID:Protective effect of acidic mannan fraction of bakers' yeast against Staphylococcus aureus infection in mice. 391 89

The minor teichoic acid linked to glycopeptide was isolated from lysozyme digests of Bacillus coagulans AHU 1631 cell walls, and the structure of the teichoic acid moiety and its junction with the peptidoglycan were studied. Hydrolysis of the teichoic-acid--glycopeptide complex with hydrogen fluoride gave a nonreducing oligosaccharide composed of glucose, galactose and glycerol in a molar ratio of 3:1:1 which was presumed to be dephosphorylated repeating units of the polymer chain. From the results of structural analysis involving NaIO4 oxidation, methylation and acetolysis, the above fragment was characterized as glucosyl(beta 1----3)glucosyl(beta 1----6)galactosyl(beta 1----6)glucosyl(alpha 1----1/3)glycerol. In addition, the Smith degradation of the complex yielded a phosphorus-containing fragment identified as glycerol-P-6-glucosyl(beta 1----1/3)glycerol. These results led to the most likely structure for the repeating units of the teichoic acid, -6[glucosyl(beta 1----3)]glucosyl(beta 1----6)galactosyl(beta 1----6)glucosyl(alpha 1----1/3)glycerol-P-. The minor teichoic acid, just like the major teichoic acid bound to the linkage unit, was released by heating the cell walls at pH 2.5. The mild alkaline hydrolysis of the minor teichoic acid after reduction with NaB3H4 gave labeled saccharides characterized as glucosyl(beta 1----6)galactitol and glucosyl(beta 1----3)glucosyl(beta 1----6)galactitol, together with a large amount of the unlabeled repeating units of the teichoic acid chain. Thus, the minor teichoic acid chain is believed to be directly linked to peptidoglycan at the galactose residue of the terminal repeating unit without a special linkage sugar unit.
...
PMID:Structural studies on the minor teichoic acid of Bacillus coagulans AHU 1631. 395 96

Biochemical parameters (dry matter, DNA, protein, cAMP, and calmodulin) were measured in tibial dyschondroplastic (TD) cartilage. This abnormal cartilage, which is a mass of unmineralized, unvascularized cartilage found in the proximal metaphysis of the tibiotarsus and tarsometatarsus, was compared with normal epiphyseal growth plate and hypertrophic cartilage obtained from day-old embryonic cone. The latter tissue is an example of cartilage which rapidly undergoes vascularization and mineralization. When compared with normal growth plate, tibial dyschondroplastic cartilage was found to contain lower amounts of dry matter, DNA, protein, cAMP, and calmodulin. This cartilage did not respond to factors in serum which stimulate 35S uptake. Although the above two types of cartilage contained similar amounts of ash, TD cartilage had less phosphorus and potassium and more sodium than the growth plate. The two types of cartilage had similar lysozyme activity and proteoglycan (hexosamine) content. In many of the parameters measured, day-old hypertrophic cartilage was similar to the normal growth plate. However, these tissues did differ in DNA, protein, ash, and lysozyme content. Substantially greater amounts of ash and lysozyme were found in the hypertrophic cartilage, which appeared to be related to events of mineralization and vascularization of this cartilage. These events did not occur in the abnormal cartilage cells found in the tibial dyschondroplastic lesion.
...
PMID:Avian tibial dyschondroplasia. II. Biochemical changes. 399 38

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.
...
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 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.
...
PMID:Structure and immunological specificity of the Streptococcus mutans group b cell wall antigen. 412 3

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.
...
PMID:Extraction, purification, and chemical and immunological properties of the Streptococcus mutans group "a" polysaccharide cell wall antigen. 419 54

The particulate hydrogenase of Vibrio succinogenes is solubilized during treatment of cell envelopes at pH 11.0. Alkali-solubilized enzyme requires sulfhydryl compounds for activity. At neutral pH, soluble enzyme is reincorporated into alkalitreated cell envelopes and no longer requires an additional activator. In the present study, cell envelopes prepared by lysing cells with ethylenediaminetetraacetic acid plus lysozyme (EDTA-lysozyme) were used to determine the chemical composition of cell envelopes and derived pH 11.0 soluble and insoluble fractions and to investigate some properties of the binding and activation of alkali-solubilized hydrogenase. Lysis with EDTA-lysozyme resulted in the formation of spheroplast ghosts. The derived cell envelopes contained 61% protein, 3% ash, 23% lipid, and 1% phosphorus. The alkali-treated cell envelopes contained 50% protein, 2% ash, 24% lipid, and 1% phosphorus. The ash from cell envelopes and alkali-treated cell envelopes was rich in iron and phosphorus and also contained calcium, copper, magnesium, sodium, and zinc. Virtually all of the weight of the ashed samples was accounted for by the oxides of these metals. Since the reconstitution of particulate hydrogenase was achieved with pH 11.0 supernatant solution and precipitate, intact mucopeptide is not essential for hydrogenase binding. Release of hydrogenase during EDTA-lysozyme lysis was found to depend upon an apparent structural change which occurs in the membranes during extended storage at -20 C.
...
PMID:Chemical constituents and hydrogenase binding in cell envelopes of Vibrio succinogenes. 497 63

A procedure for the isolation and purification of competence factor produced in a defined medium by group H streptococci, strain Challis-6, is presented. Partial characterization and chemical analysis of the product are described. The procedure yields competence factor of high purity, as shown by homogeneity in electrofocusing, by electrophoresis in sodium dodecyl sulfate polyacrylamide gels, and by chemical analysis. The data indicate that competence factor is a small, dialyzable, highly basic compound. It is free from lipids, phosphorus, and carbohydrates, and is colorless and thermoresistant. Its biological activity is destroyed by trypsin but not by deoxyribonuclease, ribonuclease, lipase, or lysozyme. Its high isoelectric point of above pH 11.0 suggests that competence factor may be a protamine or a polymer of basic amino acids. The possibility that a polyamine may be an integral part of the polypeptide molecule has not been excluded.
...
PMID:Purification and properties of Streptococcal competence factor isolated from chemically defined medium. 501 23

The spore appendages of Clostridium taeniosporum NI were removed from the spores by sonic treatment and were isolated by using discontinuous sucrose gradients. The amino acid composition of the appendages, which are elaborations of the spore coat, was similar to but not identical with the amino acid composition of the coats. Approximately 80% of the appendage dry weight was composed of 17 common amino acids, whereas 68% of the spore coat dry weight was amino acids. Mole ratios of the amino acids differed between the appendages and spore coats. The appendages contained neither diaminopimelic acid nor hydroxyproline. Glucosamine was an abundant constituent but muramic acid was absent. Approximately 10% of appendage dry weight consisted of three sugars, one of which was glucose. Phosphorus content was high and dipicolinic acid was absent. Appendage fine structure was not affected by common buffers, dilute acids and bases, hydrogen bond-breaking agents, certain proteolytic enzymes, or lysozyme.
...
PMID:Isolation and partial chemical characterization of the spore appendages of Clostridium taeniosporum. 505 56

1. After extraction of teichoic acid from cell walls of Bacillus licheniformis with dilute alkali, the insoluble residue contains the teichuronic acid and mucopeptide components and a small amount of residual phosphorus. 2. A complex of teichuronic acid and a part of the mucopeptide was isolated from the soluble fraction obtained by lysozyme treatment of alkali extracted walls. 3. Small-molecular-weight mucopeptide fragments, not containing teichuronic acid, are obtained from the soluble fraction in yields similar to those obtained after treatment of whole walls or acid-extracted walls with lysozyme. 4. The covalent linkages between teichuronic acid and mucopeptide are broken by treatment with dilute acid. The release of teichuronic acid chains is accompanied by the hydrolysis of N-acetylgalactosaminide linkages and the exposed N-acetylgalactosamine residues form chromogen under very mild conditions, indicating that they are substituted on C-3. 5. The initial rate of formation of reactive N-acetylgalactosamine residues during mild acid hydrolysis is parallel to the rate of extraction under the same conditions of teichuronic acid from alkali-treated insoluble walls, and to the rate of acid hydrolysis of glucose 1-phosphate. 6. The results suggest that the teichuronic acid chains are attached through reducing terminals of N-acetylgalactosamine residues to phosphate groups in the mucopeptide. 7. Muramic acid phosphate was isolated from the insoluble mucopeptide remaining after extraction of walls with dilute alkali followed by dilute acid.
...
PMID:The cell wall of Bacillus licheniformis N.C.T.C. 6346. Linkage between the teichuronic acid and mucopeptide components. 541 40


<< Previous 1 2 3 4 5 6 Next >>

---