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)

Chromatography of honeybee venom on Sephadex G-150 super fine revealed a high molecular weight (HMW) fraction that elutes prior to hyaluronidase (HYAL) and comprises 2% to 4% of the venom weight. HMW appears to exist in polymeric form, and the polymer which is present in greatest concentration has an estimated molecular weight of 105,000 D. The 12% nitrogen content of HMW suggests it may not be all protein. HMW is antigenically and enzymatically distinct from HYAL and phospholipase A2 (PHOS A). The acid phosphatase activity known to be present in honeybee venom was found in the HMW fraction. Since it reacts by RAST with the sera of most individuals known to be sensitive to honeybee venom, and releases histamine from the peripheral leukocytes of such individuals, its role as an allergen is confirmed. Since individuals react to different degrees to HMW, HYAL, and PHOS A, there does not appear to be a single principal allergen in honeybee venom.
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PMID:A high molecular weight allergenic fraction of honeybee venom. 7 Apr 36

The mammalian toxicity of the potently algogenic venom of the ant Pogonomyrmex badius is greater than that reported for any other insect venom. This enzyme-rich venom contains high concentrations of phospholipase A2 and B, hyaluronidase, acid phosphatase, lipase, and esterases. This hemolytic secretion from the poison gland products unusual symptoms in mammals and appears to have been evolved as a deterrent for vertebrate predators.
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PMID:A harvester ant venom: chemistry and pharmacology. 65 54

Africanized honeybees (HBs) pose a hazard to both normal and sting-sensitive subjects in certain areas of Central and South America, and it is predicted that they will soon be present in the southern United States as well. Using an electrical stimulation device, we collected Africanized HB venom (AHV) in Venezuela and European HB venom (EHV) in Louisiana. These venoms, along with commercial European HB venom (CHV), were compared by thin-layer isoelectric focusing and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The Coomassie brilliant blue and silver-stained banding patterns of AHV and EHV were essentially identical to CHV. Western blots were prepared from SDS-PAGE gels and tested with pooled sera from EHV-sensitive subjects and then radiolabeled antihuman IgE. The resulting autoradiographs revealed similar banding patterns among EHV, AHV, and CHV. RAST-inhibition studies were performed with solid-phase CHV and pooled sera from EHV-sensitive subjects. The specific allergenic activities of the three HB venoms (allergy units per milligram of protein) were comparable. By RAST-inhibition assay with solid-phase, highly purified individual venom components, AHV and EHV both contained phospholipase A2, hyaluronidase, and high-molecular-weight allergens. The increased morbidity after Africanized HB stings is likely related to their more defensive behavior during which many bees react by stinging rather than to biochemical or allergenic differences between AHV and EHV.
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PMID:Biochemical and immunochemical comparison of Africanized and European honeybee venoms. 229 9

Acid phosphatase from bee venom was purified by a combination of saturated ammonium sulphate precipitation, gel filtration and ion exchange chromatography. The final product which is a glycoprotein contained less than 0.1% phospholipase A2 or hyaluronidase activity and existed in two molecular weight (96,000 and 45,000) forms. Acid phosphatase is a potent allergen, in bee venom allergic patients, which is capable of releasing histamine from sensitized human basophils and of inducing a wheal and flare reactions in sensitized human skin.
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PMID:The purification of acid phosphatase from honey bee venom (Apis mellifica). 342 90

Classical techniques for studying modulations of microvascular permeability have a time resolution of minutes. A newly developed method allows continuous measurement of the electrical resistance of the microvascular membrane in vivo (Olesen & Crone 1983). The technique exploits microelectrodes impaled into the vascular lumen and is based on cable analysis of the vessel. It was applied to venules on the surface of the frog brain to test the effect on microvascular permeability of a wide variety of substances. The following agents increased ionic permeability reversibly within seconds: 5-hydroxytryptamine, bradykinin, ATP, ADP, AMP, phospholipase A2, arachidonic acid, leukotriene C4, oxygen-derived free radicals, ionophore A23187, and unbound Evans blue dye. An irreversible permeability increase was induced by protamine sulphate, neuraminidase, trypsin, melittin, and snake venoms from Crotalus durissus terrificus and Bothrops atrox. The following substances were without effect within an administration period of 5 min: histamine, epinephrine, putrescine, angiotensin II, vasoactive intestinal polypeptide (VIP), substance P, neurotensin, vasopressin, adenosine, PGE2, PGF2 alpha, prostacyclin (PGI2), leukotriene B4, albumin, heparin, plant cytokinins, hyaluronidase, thrombin, wasp venom. Variations in pH between 5.1 and 8.6 did not change permeability. Three conclusions are drawn from the observations: (1) the permeability of cerebral microvessels can be modulated by specific agents, (2) the agents induced changes in the endothelium within a few seconds, and (3) the rapid permeability increase induced by inflammatory mediators was less than two-fold and reversible within minutes.
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PMID:Substances that rapidly augment ionic conductance of endothelium in cerebral venules. 348 16

The large apical segments of guinea pig sperm acrosomes were mechanically separated from the spermatozoa and subsequently isolated by density gradient centrifugation. The isolated acrosomal caps were very stable and maintained their crescent morphology when suspended in sucrose-based medium buffered at pH 5.6, with or without the acrosin inhibitor p-aminobenzamidine (pAB). Examination under the electron microscope showed that the acrosomal caps were free of plasma membrane and were bound by an outer acrosomal membrane which was discontinuous. Enzymatic analysis after lysis of the caps indicated that acrosin and hyaluronidase were present with high specific activity, while only a trace amount of acid phosphatase activity and no arylsulphatase, phospholipase A2, or phospholipase C activities were present. Significant particulate acrosin activity, but only trace amounts of soluble acrosin activity, could be detected in the isolated acrosomal caps if assayed immediately after isolation in the absence of pAB. However, soluble acrosin activity of high specific activity was obtained after the acrosomal caps were extracted by 10% glycerol buffered at low pH (pH 3.0). The new procedures provide a means to isolate and purify guinea pig sperm apical acrosomal segments rapidly.
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PMID:Isolation of a stable apical segment of the guinea pig sperm acrosome. 350 56

We have measured in allergic and non-allergic beekeepers IgE and IgG antibodies to the bee venom allergens, phospholipase A2 (PLA2) and hyaluronidase (HYAL), by the radioallergosorbent test (RAST) and a 125I-radiolabelled antigen-binding assay. The absolute amount of IgG antibody in a reference serum was determined by saturation analysis using 125I-radiolabelled PLA2 and HYAL. Using monoclonal anti-IgE coated microtitre plates, the absolute amount of IgE antibody to the same antigen was also determined by saturation analysis. Regardless of the IgE response to the different allergens, IgG antibody concentrations to PLA2 were invariably higher than those to HYAL. In addition, the ratio of IgG to IgE antibody was higher for PLA2 (220:1) than for HYAL (10:1). Higher levels of IgG antibody to both allergens (especially HYAL) were found in those who had had prolonged exposure to bee stings. These data suggest that the level of IgG antibody produced is related to the dose administered, while the amount of IgE antibody may be regulated by other factors.
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PMID:Immune response to bee venom. II. Quantitation of the absolute amounts of IgE and IgG antibodies by saturation analysis. 358 9

We have developed a sensitive enzyme-linked immunosorbent assay (ELISA) which measures antibodies to bee venom phospholipase A2 (PLA2) and hyaluronidase (HYAL), horse IgG, bovine casein, and the bacterium Streptococcus mutans in each of the four human IgG subclasses. For this purpose, we have used mouse monoclonal antibodies (McAb) specific for each subclass and one which showed 'pan-IgG' reactivity. Binding to human IgG was similar for all the McAb and dilution of human IgG resulted in similar dilution curves for each subclass. Results were expressed as arbitrary U ml-1 by comparing the optical density obtained with each subclass-specific McAb to a reference curve for total IgG antibody constructed using the 'pan-IgG' McAb. Close agreement was found between the total amount of IgG antibody and the sum of the antibody in each of the four subclasses (PLA2 r = 0.90, horse IgG r = 0.98, bovine casein r = 0.84, S. mutans r = 0.85), confirming that these assays provide semi-quantitative measurements of the amount of subclass-specific antibody.
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PMID:Development of a semi-quantitative enzyme-linked immunosorbent assay (ELISA) for detection of human IgG subclass antibodies. 380 34

We have developed a sandwich enzyme-linked immunosorbent assay (ELISA) for measurement of IgE antibodies to the bee venom allergens phospholipase A2 (PLA2) and hyaluronidase (HYAL). The assay is 10-20 times more sensitive than conventional indirect ELISA or radioallergosorbent test (RAST). Furthermore, by using affinity purified rabbit antibodies to these allergens, the specificity of the test was increased compared to RAST. The use of antibodies to link the antigen to the solid phase removes the dependence on the individual protein's ability to bind to the microtitre plate. The increased sensitivity of the sandwich assay seems to be due to better presentation and retention of antigen on the solid phase.
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PMID:Increased sensitivity and specificity of a sandwich ELISA for measurement of IgE antibodies. 388 2

An enriched fraction of human decidual cells that synthesizes and releases human PRL (hPRL) was obtained by isopycnic centrifugation of collagenase- and hyaluronidase-dispersed cells through Percoll. The cells that synthesized and released hPRL banded at a density of 1.017-1.045 g/ml, an area of the gradient comprising only a small percentage of the total decidual DNA. The enriched cells formed distinct colonies in culture and contained hPRL, as evidenced by indirect immunofluorescent staining with anti-PRL serum. Plated at a density of 5.0 x 10(5) cells/well, the cells produced hPRL at a mean rate of 8.1 +/- 1.1 ng/microgram DNA . 24 h (mean +/- SD) for 8 days. Like decidual explants, the enriched cells responded to phospholipase A2 (0.1 U/ml) with a 54% decrease in hPRL release and to placental conditioned medium (0.5 mg protein/ml medium) with a 62% increase. Insulin (8.3 x 10(-7) M), progesterone (10(-5) - 10(-12) M), and estradiol (10(-5) - 10(-12) M) did not affect hPRL release over 6 days. These results indicate that enriched PRL-releasing cells, obtained by the isopycnic centrifugation of collagenase- and hyaluronidase-dispersed cells, are a useful model for the study of the synthesis and release of PRL.
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PMID:Characterization of the synthesis and release of prolactin by an enriched fraction of human decidual cells. 630 Jan 79


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