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)

Mycobacterium ulcerans produces an exotoxin in culture which, when inoculated into guinea pig skin, causes inflammation, necrosis, edema, and other histopathological changes resembling those in infections of humans. The toxin was resistant to heat and to alkalies and was moderately acid labile. Toxic activity was destroyed by Pronase, phospholipase, lipase, amylase, and glucosidase but not by trypsin, collagenase, cellulase, lysozyme, hyaluronidase, or neuraminidase. Toxic activity was resistant to treatment with 2-mercaptoethanol, urea, guanidine hydrochloride, p-chloromercuribenzoate, ethylenediaminetetraacetate, and sodium deoxycholate but was destroyed by sodium m-periodate and sodium dodecyl sulfate. The toxin was precipitated by a wide range of ammonium sulfate concentrations. Extraction with chlorofrom-methanol or petroleum ether destroyed its activity. Isopycnic density gradient ultracentrifugation in KBr produced a high-density lipoprotein layer with a 24-fold increase in specific activity. The results indicate that this toxin is a high-molecular-weight phospholipoprotein-polysaccharide complex.
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PMID:Further characterization of Mycobacterium ulcerans toxin. 3 Jun 94

Guinea-pig epidermal cells in culture possess a glycocalyx coat similar to that in vivo, as revealed by the ruthenium red stating technique. Trypsin, phospholipase C, and lysozyme do not produce any changes of the glycocalyx, while hyaluronidase and neuraminidase lead to partial and subcomplete removal respectively. Cells stripped of their glycocalyx coat by neuraminidase do not detach from the support and do not show any signs of toxicity. There is complete reconstitution of the glycocalyx within 24 hr.
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PMID:Glycocalyx of epidermal cells in vitro: demonstration and enzymatic removal. 4 27

The ultrastructural study of liver tissues from 38 patients with type B viral hepatitis consistently showed the presence of hepatitis B core antigen of 21-25 nm size in the liver cell nuclei and to a lesser extent in the cytoplasm. This finding and the demonstration of the tubular form of hepatitis B surface antigen in the proliferative degranulated endoplasmic reticulum constituted the etiologic criterion for the diagnosis of the disease. The double-shelled Dane-like particles were frequently found in association with the tubular form of the surface antigen. The core particles were found in the protoplasmic processes of hepatocytes and this correlated with the immunofluorescent microscopic findings that the antigen may be shed into circulation with the protoplasm. The core antigen was found to resist digestion by various enzymes such as protease, DNase, RNase, phospholipase C, lipase, lysozyme, diastase, neuraminidase and hyaluronidase, all of which did not destroy the immunoreactivity as demonstrated by immunoelectron and immunofluorescent microscopy. Similarly, sodium dodecyl sulfate, Tween 80 and mercaptoethanol also had no effect. The formalin-fixed paraffin-embedded liver tissue sections could be treated with protease to facilitate the immunofluorescent staining for the core antigen in tissue.
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PMID:Structural and immunoreactive characteristics of hepatitis B core antigen. 5 6

The purification procedure for endo-beta-N-acetylglucosaminidase D was improved to yield an enzyme preparation which was homogeneous upon gel electrophoresis. The molecular weight of the enzyme as estimated by Sephadex G-200 column chromatography was 280,000, while SDS-gel electrophoresis after reduction with 2-mercaptoethanol gave a value of 150,000. The purified enzyme did not show any chitinase, hyaluronidase or lysozyme activity. In the presence of exoglycosidases removing peripheral sugars, the endoglycosidase acted on serum glycoproteins such as transferrin and fetuin. The enzyme also hydrolyzed an oligosaccharide, (Man)5(GlcNAc)2, indicating that the peptide portion of substrates does not have much effect on susceptibility to the enzyme.
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PMID:Further studies on endo-beta-N-acetylglucosaminidase D1. 7 85

1. An activator catalysing specifically conversion of latent forms of human leucocyte collagenase and gelatin-specific protease into the active forms, has been isolated from rheumatoid synovial fluid and purified 55-fold with a yield of 16%. 2. Molecular weight of the activator is about 35 000. 3. The activator is thermolabile, and is irreversibly inactivated at pH below 5.5 or in the presence of low concentrations of trypsin or papain; it is resistant to the action of lysozyme, hyaluronidase, diisopropylfluorophosphate, soybean trypsin inhibitor, p-chloromercuribenzoate, iodoacetamide and dithiothreitol. 4. The activator did not show any activity towards collagen, gelatin, casein, haemoglobin, histones, elastin or p-phenylazobenzyloxycarbonyl-peptide.
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PMID:Isolation, purification and properties of a factor from rheumatoid synovial fluid activating the latent forms of collagenolytic enzymes. 17 Jul 64

Optimal conditions for detecting staphylokinase, phosphatase, protease, lipase, esterase, egg yolk factor, lysozyme, deoxyribonuclease, hyaluronidase, penicillinase, and alpha-, beta-, and delta-hemolysins in cell-free filtrates of selected strains of staphylococci by agar plate methods were established by studying the effect of factors such as buffer composition, pH, ionic strength, type of agar, nature and concentration of substrate, and certain metal ions. The final tests that evolved from this study are simple to perform, require only 6 mul of the sample per test, and are capable of detecting microgram and, in some cases, nanogram quantities of the product. The zones of reaction can also be quantitatively related to the amount of material present. The test may also be useful for the detection of extracellular products of other microorganisms.
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PMID:Agar plate tests of enhanced sensitivity for detecting biologically active products of staphylococcal filtrates. 18 61

The extracellular production of hyaluronidase and chondroitin sulfatase was demonstrated in all of the subspecies of Bacteroides fragilis tested with the exception of B. fragilis subsp. vulgatus. Elastase was found only in one strain of B. coagulans tested. This appears to be the first report of these enzyme activities in this genus. Additional enzymes found to be produced by certain members othis genus were fibrinolysin, penicillinase, lysozyme, lecithinase, deoxyribonuclease, phosphatase, protease, and lipase.
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PMID:Extracellular enzymes of the genus Bacteroides. 18 84

Three methods at present available for the purification of staphylococcal delta-haemolysin were compared as to the purity and identify of the product obtained. None yielded a pure preparation of delta-haemolysin; one of the three preparations did not contain demonstrable delta-haemolysin when tested electrophoretically, but it contained deoxyribonuclease, penicillinase, phosphatase and alpha-haemolysin. The second preparation had delta-haemolysin activity and was free of alpha-haemolysin, but it contained lipase, egg-yolk factor, esterase, deoxyribonuclease, penicillinase, phosphatase and hyaluronidase. The third preparation contained all of the products mentioned above, except phosphatase, and it also contained alpha-haemolysin, staphylokinase, lysozyme and caseinase. These findings are discussed with special reference to the requirement for criteria of purity in work with staphylococcal products.
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PMID:Purity of staphylococcal delta-haemolysin obtained by three different procedures. 18 51

Further investigation with the inhibitor of interferon activity (IME) isolated from mouse embryo tissue is reported. The present results bring some new data concerning the physiochemical properties of the interferon antagonist. It is not dialysable, not sensitive to trypsin, lysozyme, hyaluronidase, RNAse and pH 2, but is sensitive to pH 10 and neuraminidase. Concentrated and partly purified tissue antagonist of interferon was separated on a column with Sephadex G 100. Three distinct, well separated fractions showing antiinterferon activity were obtained. The characteristics and molecular weight of each of these fractions were determined.
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PMID:Physicochemical characteristics of IME-inhibitor of interferon activity from mouse embryo tissues. 20 16

Anionic sites on the surface of Brucella canis were visualized in the electron microscope by staining with positively charged ferric oxide hydrosols in acetic acid (AI-reagent), or propanoic acid (PI-reagent), and with a polycationic ferritin derivative. With the AI-reagent, single or small aggregates of ferric oxide particles were bound to the cell surface of Br. canis, whereas, with the lipophilic PI-reagent, the microorganisms were heavily stained with focal aggregates of iron granules. The polycationic ferritin label was uniformly distributed over the entire cell surface of Br. canis. The ferritin label was not bound on the surface of the organisms after prior treatment with trichloroacetic acid or methanolic hydrochloric acid. Treatment with aqueous acetone, chloroform/methanol, diethyl ether, sodium deoxycholate, pronase, lysozyme, hyaluronidase, and sodium periodate neither influenced the morphology of the Brucella nor diminished their ionic binding sites. Our results indicate that the anionic sites on the cell surface of Br. canis may be carboxyl and phosphate groups of lipopolysaccharides.
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PMID:[Ultrastructural investigations on anionic surface sites of Brucella canis (author's transl)]. 60 17


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