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)

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

A homogeneous population of single cells from the thick ascending limb of Henle's loop (TALH) has been isolated from the rabbit kidney medulla. A total medullary cell suspension was prepared by a series of collagenase, hyaluronidase, and trypsin digestions and separated on a Ficoll gradient (2.6-30.7% wt/wt). Morphologically, the cells isolated from the TALH were homogeneous and showed polarity within their plasma membrane structure, with a few blunt microvilli on their apical surface and deep infoldings of the basal-lateral membrane. Biochemically, the TALH cells were highly enriched in calcitonin-sensitive adenylate cyclase and Na, K-ATPase. Alkaline phosphatase and arginine vasopressin-sensitive adenylate cyclase, highly concentrated in proximal tubule and collecting duct, were present only in low concentrations in the TALH cells. Additionally, furosemide, a diuretic inhibiting sodium chloride transport in the TALH in vivo, inhibited oxygen consumption of the TALH cells in a dose-dependent manner. The TALH cells were viable, as judged by morphological appearance, trypan blue exclusion, the response of oxygen consumption to 2,4-dinitrophenol, succinate and ouabain, and the cellular Na, K and ATP levels.
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PMID:Separation of renal medullary cells: isolation of cells from the thick ascending limb of Henle's loop. 625 27

Several techniques for assaying and localizing hyaluronan (HA), all based on the affinity to hyaluronan of proteins isolated from cartilage, chondrosarcoma, or brain, have been proposed. We show here that a unique reagent, alkaline phosphatase-linked hyaluronectin, can be used to assay hyaluronan in biological fluids or tissue extracts (enzyme-linked sorbent assay method) and to characterize it in cells or tissue sections in two steps: reagent incubation and staining. Results of assays in biological fluids or tissue extracts showed a good correlation with results of the previously described technique using antibodies to detect hyaluronectin bound to a plastic microtest plate (B. Delpech et al., 1985, Anal. Biochem. 149, 555-565) for both low concentrations (< 1 mg/liter, r = 0.973, P < 0.001) and high concentrations (> 1 mg/liter, r = 0.953, P < 0.001). The interassay variations were 8.5% when the assay was performed at 4 degrees C and 18.5% at 37 degrees C. The intraassay variations under those conditions were, respectively, 14.4 and 6.5%. Tissue HA could be detected easily with the reagent, as shown in fetal tissues and in tumors. Specificity of the reaction was controlled either by blocking the reagent with an excess of hyaluronan (which was not possible with other glycosaminoglycans) or by destroying tissue hyaluronan with streptomyces hyaluronidase. Alkaline phosphatase-linked hyaluronectin was also used to assay hyaluronidase activity in several biological fluids. One-hour incubation of hyaluronidase preparations on HA-coated plates made it possible to detect as low as 1 mU bovine testis hyaluronidase and 0.1 mTRU streptomyces hyaluronidase. Four-hour incubation made it possible to detect activity in a 1/12,500 dilution of human serum.
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PMID:Enzyme-linked hyaluronectin: a unique reagent for hyaluronan assay and tissue location and for hyaluronidase activity detection. 853 92