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

The purpose of the present study was to determine the surface hydrophobicity of small oral spirochetes and to receive an impression of the molecular organization of the cell surfaces. Nine spirochete strains with one endoflagellum from each cell-end (1:2:1 spirochetes) and eight with two endoflagella from each cell-end (2:4:2 spirochetes) from subgingival plaque were examined. Two hydrophobicity assay systems were used: 1) two-phase partitioning and 2) salting-out aggregation by ammonium sulfate. The influence of heat, enzymes, saliva, and serum were examined. The 2:4:2 spirochetes were significantly more hydrophobic than the 1:2:1 spirochetes. For all strains heat treatment increased surface hydrophobicity, whereas incubation with proteases decreased surface hydrophobicity for the 1:2:1 spirochetes. The 2:4:2 spirochetes were unaffected by the proteases. Lipase and hyaluronidase affected the two morphotypes in opposite directions. Saliva did not affect the surface hydrophobicity of any of the strains, whereas rabbit serum decreased this property for the 2:4:2 strains.
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PMID:Surface hydrophobicity of small oral spirochetes. 202 70

Venoms from 20 species of stinging Hymenoptera, including nine species of ants and nine species of social wasps, were quantitatively analyzed for the following enzymic activities: phospholipase A, hyaluronidase, lipase, esterase, protease, acid phosphatase, alkaline phosphatase and phosphodiesterase. Phospholipase and hyaluronidase were present in all the venoms, with activity levels generally higher among the wasps than the ants (P less than 0.05). Lipase was present in high activity in several social wasp venoms and one ant venom, in low levels in two other ant venoms and absent from four tested snake venoms. Two-carbon esterase activity was present in the venoms of five social wasps and one ant. Non-specific protease was present at very high activity levels in the venoms of an army ant species and was also present in the venoms of a social wasp and another ant. Acid phosphatase activity was present in eight of the nine ant venoms, but was essentially absent from all the social wasp venoms. Alkaline phosphatase activity was clearly detectable in the venoms of only two species of ants. Phosphodiesterase, an enzyme not previously detected in insect venoms, was present in the venoms of three closely related ant species. Venoms with generally high enzymic activities included those of Polistes infuscatus, Vespula (V.) squamosa and Pogonomyrmex badius; those with low activities included Dolichovespula maculata, Apoica pallens and Dasymutilla lepeletierii. The 20 venoms were ranked according to overall activity levels using the eight enzyme activities plus lethal, hemolytic and pain-inducing activities. They were also compared phylogenetically using these 11 activities.
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PMID:Comparative enzymology of venoms from stinging Hymenoptera. 354 39