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)

The catalytic activities of lysozyme, horseradish peroxidase (HP), catalase, glucose-6-phosphate dehydrogenase (G6PDH) and lactate dehydrogenase (LDH) were studied in aqueous solutions and after isolation of the enzymes from mixed reversed micelles of Aerosol OT and Triton X-45 by organic solvents (acetone, ethanol, isopropanol), by acetone-water mixtures, as well as by aqueous solutions containing urea, glycerol, polyethylene glycol 6000 and ammonium sulphate. The isolation conditions were found for catalase with retaining all the activity and for HP and lysozyme with retaining 72 and 84% of the catalytic activity, respectively. The G6PDH isolation from micelles by aqueous solutions of urea (6%) and glycerol (10%) resulted in retaining only 43% of the enzyme activity and led to almost complete inactivation of LDH. Stability of the enzymes after their entrapment in micelles and isolation from those is compared with thermostability of the same enzymes in aqueous solutions.
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PMID:[Isolation of enzymes from mixed reversed micelles of surface-active agents]. 245 51

Commercial Streptomyces griseus and Serratia marcescens chitinases and purified wheat germ W1A and hen egg white lysozymes were subjected to polyacrylamide gel electrophoresis under native conditions at pH 4.3. After electrophoresis, an overlay gel containing 0.01% (W/V) glycol chitin as substrate was incubated in contact with the separation gel. Lytic zones were revealed by uv illumination with a transilluminator after staining for 5 min with 0.01% (W/V) Calcofluor white M2R. As low as 500 ng of purified hen egg lysozyme could be detected after 1 h incubation at 37 degrees C. One band was observed with W1A lysozyme and several bands with the commercial microbial chitinases. The same system was also used with native polyacrylamide gel electrophoresis at pH 8.9. Several bands were detected with the microbial chitinases. The same enzymes were also subjected to denaturing polyacrylamide gel electrophoresis in gradient gels containing 0.01% (W/V) glycol chitin. After electrophoresis, enzymes were renatured in buffered 1% (V/V) purified Triton X-100. Lytic zones were revealed by uv after staining with Calcofluor white M2R as for native gels. The molecular weights of chitinolytic enzymes could thus be directly estimated. In denaturing gels, as low as 10 ng of purified hen egg white lysozyme could be detected after 2 h incubation at 37 degrees C. Estimated molecular weights of St. griseus and Se. marcescens were between 24,000 and 72,000 and between 40,500 and 73,000, respectively. Some microbial chitinases were only resistant to denaturation with sodium dodecyl sulfate while others were resistant to sodium dodecyl sulfate and beta-mercaptoethanol.
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PMID:Detection of chitinase activity after polyacrylamide gel electrophoresis. 247 67

The outer membrane of Campylobacter coli, C. jejuni and C. fetus cell envelopes appeared as three fractions after sucrose gradient centrifugation. Each outer membrane fraction was contaminated with succinate dehydrogenase activity from the cytoplasmic membrane fraction. Similarly the inner membrane fraction was contaminated with 2-ketodeoxyoctonate and outer membrane proteins including the porin(s). The separation of these two membranes was not facilitated by variations in lysozyme treatment, cell age, presence or absence of flagella, or longer lipopolysaccharide chain length. Sodium lauroyl sarcosinate extraction resulted in an outer membrane fraction which contained some inner membrane contamination and produced multiple bands upon sucrose gradient centrifugation. Triton X-100 extraction removed the inner membrane from the outer membrane and Triton X-100/EDTA treatment extracted lipopolysaccharide-rich regions of the outer membrane which contained almost exclusively the Campylobacter porin(s). These data indicated that the inner and outer membranes of the Campylobacter cell envelope were very difficult to separate, possibly because of extensive fusions between these two membranes.
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PMID:Comparison of methods used to separate the inner and outer membranes of cell envelopes of Campylobacter spp. 247 28

1. Lysozyme activity was detected after electrophoresis in sodium dodecyl sulfate-polyacrylamide gels containing 0.2% (W/V) autoclaved Micrococcus lysodeikticus cells as substrate. 2. Lysozyme activity appeared as clear lysis zones after incubation of opaque gels at 37 degrees C in buffered Triton X-100. 3. As low as 0.1 pg of purified hen egg white lysozyme could be detected after 16 hr incubation at pH 6.5. 4. Bands with lytic activity from kidney and pancreas acetone powders, bird's egg whites and vitelline membranes, animal sera and human saliva corresponded to c-type (Mr 14,500), g-type (Mr 20,500) or both lysozymes as far as molecular weight is concerned. 5. Some extracts, like porcine kidney, exhibited more than two bands. 6. Bands with lytic activity migrating at the level of g-type lysozymes were detected in some kidney and pancreas extracts.
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PMID:Lysozyme activity in animal extracts after sodium dodecyl sulfate-polyacrylamide gel electrophoresis. 270 41

Surface proteins of nine Campylobacter jejuni strains belonging to three different serovia were extracted with lysozyme/ethylenediamine-tetraacetic acid. The preparations bound to isolated murine small intestinal cells and to a membrane fraction (MF) of isolated brush borders obtained by detergent treatment with Triton X-100 and Nonidet P40. Binding was demonstrated by an enzyme-linked immunosorbent assay procedure. Using lipopolysaccharide (LPS)- and flagella-specific antisera the contribution of flagella and LPS, present in the protein preparations, to the total binding to MF was investigated. Only up to approximately 10% of the total binding of each strain was found to be mediated by LPS, 10%-33% of binding was flagella dependent. The preparations of four strains (serovar HS2) bound in a trypsin-sensitive manner (45%-85% reduction), while the others (serovaria HS1 and HS13) were hardly influenced by trypsin treatment. Binding to MF was not impaired by preincubation of the bacterial surface protein preparations with several sugars and lectins.
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PMID:In vitro binding of Campylobacter jejuni surface proteins to murine small intestinal cell membranes. 274 90

A simple technique is proposed for detection of bacterial restriction endonucleases. Analysis is performed directly in the cells from colonies cultivated on Petri dishes. The cells collected with an inoculation loop are treated with lysozyme and Triton X-100. After centrifugation the supernatant is tested for endonuclease activity. The technique enables up to 100 colonies to be tested for 3-4 h.
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PMID:[A method for detecting restriction endonucleases in bacterial colonies]. 283 59

Direct evidence has been obtained that the tail-associated lysozyme of bacteriophage T4 (tail-lysozyme) is gp5, which is a protein component of the hub of the baseplate. Tails were treated with 3 M guanidine hydrochloride containing 1% Triton X-100, and the tail-lysozyme was separated from other tail components by preparative isoelectric focusing electrophoresis as a peak with a pI of 8.4. The molecular weight as determined from sodium dodecyl sulfate electrophoresis was 42,000. The tail-lysozyme was unambiguously identified as gp5 when the position of the lysozyme was compared with that of gp5 of tube-baseplates from 5ts1/23amH11/eL1ainfected Escherichia coli cells by two-dimensional gel electrophoresis. The tail-lysozyme has N-acetylmuramidase activity and the same substrate specificity as gene e lysozyme; the optimum pH is around 5.8, about 1 pH unit lower than for the e lysozyme. We assume that the tail-lysozyme plays an essential role in locally digesting the peptidoglycan layer to let the tube penetrate into the periplasmic space. The tail-lysozyme is presumably also responsible for "lysis from without."
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PMID:Isolation and characterization of the bacteriophage T4 tail-associated lysozyme. 315 5

High-molecular-weight polymers of alpha-1,6-linked D-glucans are insoluble in alcohol solutions. Whole, but not parotid, saliva prevented the precipitation of D-glucans by 80% (vol/vol) ethanol, showing that the whole saliva contained a factor which complexed with the glucan to render it alcohol soluble. The glucan-binding factor was retained on a column of Sephacryl S-200 which had been preequilibrated with 80% ethanol. The factor was then eluted with water. Passive hemagglutination assays revealed that the glucan-binding factor could sensitize erythrocytes to agglutination with anti-poly(glycerolphosphate), suggesting that the active glucan-binding component with lipoteichoic acid. The glucan-solubilizing factor was resistant to heat (100 degrees C), proteases, sialidase, lysozyme, lactoperoxidase, trichloroacetic acid, and Triton X-100. When sucrose was added to saliva, a suspension of Streptococcus cricetus AHT, or a suspension of Streptococcus sanguis 10556, relatively large amounts of glucan-binding factor were released in a soluble form. In addition, penicillin G caused the release of the glucan-solubilizing component from a suspension of S. cricetus AHT. It is suggested that whole saliva contains a component, tentatively identified as lipoteichoic acid, which can complex with glucans in a relatively hydrophobic solvent. This type of complex formation may be important in the adhesion of oral streptococci to saliva-coated surfaces.
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PMID:Glucan-binding factor in saliva. 316 92

A Staphylococcus epidermidis isolate designated strain 115, which is used as an interfering agent against staphylococcosis of turkeys, produces a bacteriocin that was partially purified and characterized in this study. This bacteriocin diffused through agar media, but it was not found in appreciable quantities in the supernatant fluid of broth cultures. Extraction of the bacterial cells with 7 M urea, 1% sodium dodecyl sulfate, or 1% Triton X-100 caused considerable amounts of the bacteriocin to go into solution. This substance was partially purified by selective chemical extraction and by gel filtration chromatography using a Sephacryl S-300 column. This bacteriocin had two active forms: an aggregate, and a small-molecular-weight form estimated by gel filtration chromatography to be less than 6500. Activity was not affected by heat, repeated freeze-thaw cycles, pH 2 and pH 10, or a variety of proteolytic enzymes, nucleases, a lipase, and lysozyme.
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PMID:Staphylococcosis of turkeys. 4. Characterization of a bacteriocin produced by an interfering Staphylococcus. 357 99

Tolerant strains of Streptococcus faecium had higher levels of muramidase 2 and lower levels of trypsinactivable muramidase 1 than did susceptible strains. Susceptible strains lysed faster than did tolerant strains in buffer and at some antibiotic concentrations. The addition of Triton X-100 produced equal lysis rates for susceptible and tolerant cultures.
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PMID:Penicillin tolerance in Streptococcus faecium ATCC 9790. 366 76


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