Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.36 (hyaluronidase)
 4,606 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Certain strains of Moraxella bovis produce tissue-damaging enzymes which may initiate or potentiate infectious bovine keratoconjunctivitis. Thirteen reference strains of this species were characterized physiologically and screened for production of various enzymes by some conventional biochemical tests and the API ZYM system (Analytab Products, Plainview, N.Y.). All 13 strains were hemolytic. All hydrolyzed Tween 80 and Tween 85 and displayed C4 esterase, C8 esterase-lipase, and C14 lipase activities. All produced phosphoamidase and phosphatase. All were able to hydrolyze casein and gelatin. All produced leucine and valine aminopeptidases and fibrinolysin. Twelve produced hyaluronidase or were agarolytic. Three hydrolyzed chondroitin sulfate. Nine strains autoagglutinated. Five produced catalase, and two produced cystine aminopeptidase.
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PMID:Hydrolytic enzymes of Moraxella bovis. 625 99

All strains of Legionella pneumophila tested produced detectable levels of extracellular protease, phosphatase, lipase, deoxyribonuclease, ribonuclease, and beta-lactamase activity. Weak starch hydrolysis was also demonstrated for all strains. Elastase, collagenase, phospholipase C, hyaluronidase, chondroitinase, neuraminidase, or coagulase were not detected in any of these laboratory-maintained strains.
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PMID:Extracellular enzymes of Legionella pneumophila. 626 49

This paper describes a morphologic, quantitative, cytochemical study of mononuclear non lymphoid cells in knee synovial fluid in osteoarthritis and various arthritides. Morphologic criteria allow to identify among these cells various synoviocytic and monocytic subtypes with in both types, phagocytic subtypes. Quantitative study shows in arthritides an important afflux of monocytes and a hyperexfoliation of synoviocytes. In fluids with intermediate cellularity, Monocytes/Synoviocytes ratio allows the differential cytodiagnosis between osteoarthrosis and arthritis. All monocytic subtypes and especially the phagocytic one are highly significantly increased in arthritides. Synoviocytic subtypes show a lower increase, except the phagocytic one, which is not changed. Giant multinuclear synoviocytes are found in every type of disease and cannot constitute a cytodiagnosis marker. Alcian Blue and hyaluronidase treatment show hyaluronate in a few percentage of Synoviocytes. Cytoenzymologic study shows that synoviocytes and monocytes are positive in all tested hydrolases: beta Glucuronidase, Acid Phosphatase, alpha Naphthyl Acetate Esterase, these activities being always higher in synoviocytes. With peroxidase, synoviocytes are always negative, so this reaction although it marks only a minority of monocytic population can be used as an extra cytologic criterion for discrimination of mononuclear cells in synovial fluid. In these four enzymes there is no significant quantitative difference at cellular level between osteoarthrosis and arthritides. Lysosomal enzymatic activity in both monocytic and synoviocytic cells confirms their heterophagic properties. However synoviocytic heterophagy seems to be a physiological process not or few affected by inflammatory events. On the opposite, monocytic heterophagy and then macrophagic transformation of monocytes appears as a major aspect of intrasynovial inflammatory reaction. If a large majority of exfoliated synoviocytes comes from A type synovial lining cells and if they belong to Mononuclear Phagocyte System, why do they so weakly, or not, participate as phagocytes to inflammatory reaction.
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PMID:[Non-lymphoid mononucleated cells in the synovial fluid in arthrosis and various inflammatory arthropathies. Morphologic, quantitative and cytoenzymologic study]. 654 71

Ten Basidiobolus ranarum (= Basidiobolus haptosporus) strains, isolated from faeces of 102 different lower vertebrates (ectotherms) exhibited in Antwerp Zoo, or from their environment were studied for their temperature requirements, haemolysis and other enzyme activities in vitro. All isolates grew well at 25 and 37 degrees C. Three strains that produced undulated zygospore walls were haemolytic and positive for hyaluronidase. All the isolates produced urease, N-acetyl-beta-glucosaminidase, trypsin, lipase, lecithinase, gelatinase, collagenase and elastase, but failed to produce amylase, keratinase and beta-glucosidase. Three isolates failed to produce phosphatase. Only one strain failed to produce DNase. Aesculin was not hydrolysed. Chitinase activity was inconclusive. The results of this study illustrate the importance of exotic animals kept in temperate regions as carriers of potentially pathogenic organisms. In addition to the morphological characteristics, the identification can be based on enzymatic profiles. Enzymatic activity detection may help to explain the pathogenic mechanism of the fungus.
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PMID:Isolation of Basidiobolus ranarum from ectotherms in Antwerp zoo with special reference to characterization of the isolated strains. 1042 99

The high molecular weight arylamidase-alkaline phosphatase-complex from rat kidney microsomes [1] was carefully dissociated by means of treatment with several hydrolytic enzymes or by acidification. Trypsin, chymotrypsin and pronase cause a selective solubilization of the enzymes discernible at their different electrophoretic mobility in polyacrylamide gel. The lower migrating zone represents phosphatase, the faster migrating zone shows arylamidase activity (molecular weights 180,000 and 172,000, respectively). Incubation of the complex with papain, lipase, neuraminidase or hyaluronidase and incubation at acid conditions (pH optimum 5.0) in the absence of any enzyme also yields in the appearance of two protein bands. In contrast to the alkaline hydrolases the acid hydrolases, the pH 5-treatment and with a certain degree also the lipase liberate a second arylamidase zone lying in the phosphatese containing zone during polyacrylamide gel electrophoresis. Treatment with SDS and subsequent SDS-polyacrylamide gel electrophoresis also results in a dissociation of the complex, but only in one protein fragement (approx, molecular weight 205,000).
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PMID:??? 1194 35

Beining, Paul R. (The Catholic University of America, Washington, D.C.) and E. R. Kennedy. Characteristics of a strain of Staphylococcus aureus grown in vivo and in vitro. J. Bacteriol. 85:732-741. 1963.-A comparative survey was conducted on the characteristics of a strain of Staphylococcus aureus after it had been grown in vitro (VSB) and after it had been collected from the peritoneal exudate of an infected guinea pig (GSB). Both VSB and GSB strains gave the same results when studied in an extensive series of tests, including bound and soluble coagulases, bacteriophage type, antibiotic-sensitivity pattern, the usual fermentation reactions, deoxyribonucleic acid base composition, and qualitative tests for hemolysins, deoxyribonuclease, ribonuclease, staphylokinase, staphyloprotease, lipase, and phosphatase. The in vivo strain differed significantly from the in vitro strain in respiratory rate, agar gel diffusion studies, agglutinability in tube tests, virulence tests in rabbits and mice, growth on tellurite-glycine agar, susceptibility to human gamma-globulin in agar, and in the quantitative production of deoxyribonuclease, alpha-hemolysin, leucocidin, and hyaluronidase.
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PMID:CHARACTERISTICS OF A STRAIN OF STAPHYLOCOCCUS AUREUS GROWN IN VIVO AND IN VITRO. 1404 37

Chesbro, William R. (University of New Hampshire, Durham), Fred P. Heydrick, Roland Martineau, and Gail N. Perkins. Purification of staphylococcal beta-hemolysin and its action on staphylococcal and streptococcal cell walls. J. Bacteriol. 89:378-389. 1965.-After growth of bovine-derived strains of Staphylococcus aureus in a completely dialyzable medium, the beta-hemolysin in the culture supernatant fluids was purified by gradient-elution chromatography on cellulose phosphate. The purified hemolysin contained two components, demonstrable by immunodiffusion or electrophoresis, but was free from alpha-hemolysin, coagulase, Delta-hemolysin, enterotoxins A and B, glucuronidase, hyaluronidase, lipase, muramidase, Panton-Valentine leukocidin, phosphatase, and protease. The hemolysin was heat-labile and sulfhydryl-dependent, and the preparation was leukocidal for guinea pig macrophages. When rabbit red blood cell (RBC) stroma and staphylococcal or enterococcal cell walls were treated with the purified hemolysin, it liberated mucopolysaccharides from the rabbit RBC stroma, polysaccharides and mucopolysaccharides (or mucopeptides) from the staphyloccoal cell walls, and rhamnose, glucose, an unidentified monosaccharide, N-acetylglucosamine, and at least two polysaccharides from the enterococcal cell walls. The hemolytic and cell-wall degradative activities had similar thermal inactivation kinetics, pH optima, sedimentation coefficients, and chromatographic and electrophoretic mobilities; both required Mg and were inhibited by thiol-inactivating agents. Consequently, it seems likely that both activities are expressions of the same enzyme.
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PMID:PURIFICATION OF STAPHYLOCOCCAL BETA-HEMOLYSIN AND ITS ACTION ON STAPHYLOCOCCAL AND STREPTOCOCCAL CELL WALLS. 1425 4

1. Nine acid hydrolases, cytochrome oxidase, alkaline phenylphosphatase and catalase were demonstrated in 0.25m-sucrose homogenates of newborn-rat calvaria. The acid hydrolases were: acid phenylphosphatase, acid beta-glycerophosphatase, beta-glucuronidase, beta-N-acetylglucosaminidase (beta-N-acetylaminodeoxyglucosidase), acid ribonuclease and acid deoxyribonuclease, showing optimum activity at about pH5; cathepsin, beta-galactosidase and hyaluronidase, with optimum activity at about pH3.6. 2. The main kinetic characters of these enzymes have been studied and methods for their quantitative assay have been worked out. The activities present in bone are given and compared with those found in liver. 3. Acid-phosphatase activity was assayed with phenyl phosphate and beta-glycerophosphate as substrates: activities with these two substrates appeared to be due to two different enzymes. Acid phenylphosphatase is particularly labile and is readily inactivated by various physical or chemical agents.
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PMID:Studies on bone enzymes. The assay of acid hydrolases and other enzymes in bone tissue. 1674 42


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