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)

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

The study of the effect of synthetic polyelectrolites of the cationic type on benzylpenicillin resistant staphylococci showed that the cation polyelectrolites induced changes in the cell membrane permeability and increased penicillin absorption by the cells thus increasing sensitivity of the penicillin-resistant staphylococci to the antibiotic. Low inhibitory effect of the polyelectrolites with respect to penicillinase and hyaluronidase was shown. Changes in the membrane apparatus of staphylococcus cells due to the effect of polyelectrolites were found.
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PMID:[Effect of synthetic poly-electrolytes of the cationic type on staphylococcal sensitivity to benzylpenicillin]. 88 84

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

According to the genetic relationships among Gram-negative bacilli the genus Pasteurella is included with the genus Haemophilus and the genus Acinobacillus within the family Pasteurellacae. Pasteurella multocida, the type species, is responsible for the majority of human Pasteurella infections. P. multocida is a member of the normal flora in the upper respiratory tract of many mammals or birds. It causes sporadic or epidemic diseases among different animal species, particularly pneumonia and atrophic rhinitis in swine in intensive breeding stations. The most common human infection with P. multocida is a local cellulitis following dog or cat bites and scratches. Serious local complications are sometimes responsible for prolonged disability. The respiratory tract is the second human source of P. multocida isolates. The frequency of recovery of P. multocida from oropharynx of apparently healthy pig breeders suggests that respiratory pasteurellosis could be an occupational disease. The mechanisms of virulence of P. multocida are unclear. Several factors are involved: capsules preventing phagocytosis, a dermonecrotic toxin causing experimental atrophic rhinitis, hyaluronidase, neuraminidase and proteases. Penicillin is considered to be the drug of choice for Pasteurella infection. Tetracyclin is efficient for bites but has no bactericidal effect. Oxacillin, first-generation cephalosporins, macrolides and aminoglycosides have poor activities. In the case of beta-lactamase producing strains a bactericidal effect could be achieved with fluoroquinolones or third generation cephalosporins.
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PMID:[Pasteurelloses]. 777 Mar 88

A total of 10 strains each of Fusobacterium necrophorum subsp. necrophorum and Fusobacterium necrophorum subsp. funduliforme were tested for the production of 13 extracellular enzymes. DNase, alkaline phosphatase, and lipase were predominantly associated with all the strains of F. necrophorum subsp. necrophorum, with DNase not detected in any of the strains of F. necrophorum subsp. funduliforme. In addition, the strains of F. necrophorum subsp. necrophorum were generally more hemolytic than those of F. necrophorum subsp. funduliforme. Lecithinase, beta-lactamase, elastase, hyaluronidase, chondroitin sulfatase, and coagulase were not detected in any of the strains. DNase may be used to differentiate between the two subspecies.
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PMID:Comparison of extracellular enzymes of Fusobacterium necrophorum subsp. necrophorum and Fusobacterium necrophorum subsp. funduliforme. 837 Jul 61

Microbial growth in a Todd-Hewitt broth has been followed to determine the in-vitro post-antibiotic effects of penicillin in a Lancefield group A streptococcal strain. Bacteria were exposed for 2 h at 37 degrees C to 1 x MIC of penicillin. Following antibiotic removal, inactivation with penicillinase and regrowth in a drug-free broth, the duration of the effect was found to be 2.8 h. By studying the affinity of streptococci for xylene in the post-antibiotic phase we observed that the penicillin treatment had no effect on the cell surface hydrophobicity. The ability of the same streptococci to adhere to human buccal epithelial cells was greatly reduced. Streptococci exposed to penicillin produced much more deoxyribonuclease and hyaluronidase than control bacteria.
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PMID:Penicillin post-antibiotic effects on the biology of group A streptococci. 883 11