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)

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

Diagnosis and immunotherapy with venom extracts of patients sensitive to Hymenoptera stings has led to the problem of improving the standardization of Hymenoptera venom products. Current methods of standardization use the Lowry protein determination and a radial-diffusion assay for hyaluronidase activity. This study demonstrates that the results of these analyses do not always correlate with the actual quantity of allergenic protein present in the extracts. A method of standardization is examined herein that uses polyacrylamide gel electrophoresis to quantitate phospholipase A, antigen 5, and hyaluronidase, the proteins that together comprise most allergenic protein present in the venoms. Also discussed in this study is the biochemical variability of phospholipase A and antigen 5 in the venoms of the different vespid species examined.
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PMID:A qualitative and quantitative analysis of proteins found in vespid venoms. 370 Aug 91

Antibody responses to honey bee venom (HBV) were studied in 13 patients during a 4-month course of immunotherapy with monomethoxy polyethyleneglycol (mPEG) modified venom. There was a rise of HBV-specific IgG antibodies as measured by IgG-RAST in all patients and a slight decrease of IgE antibody in most of them. The IgG-antibody responses during mPEG-HBV treatment as examined by crossed radioimmunoelectrophoresis were directed to phospholipase A, hyaluronidase, acid phosphatase and to another allergen, antigen 1. Thus, despite a high degree of mPEG-modification of HBV, the immunogenicity of the most important HBV allergens was retained.
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PMID:IgG and IgE antibody patterns after immunotherapy with monomethoxy polyethyleneglycol modified honey bee venom. 370 78

Eight sequentially collected lots of aqueous extracts of imported fire ant (IFA) front end and abdominal end segments were assayed for phospholipase A (PLA), N-acetyl-beta-glucosaminidase (NAG), and hyaluronidase. Relative potency of each extract lot and pooled venom was measured by RAST inhibition against a venom standard. More than a hundredfold difference in PLA activity was observed. Early summer collections had the highest activity. The May to June collection had more than twice the PLA activity of the next most potent lot. Discordancy in enzyme patterns was noted only in AE extract. NAG levels peaked earlier in the spring and summer and fluctuated less widely. Front end extract had lower activity levels for both enzymes, with no seasonal fluctuation in NAG and a single elevation in PLA activity in the April to May collection. RAST inhibition varied directly with PLA activity (p less than .05) but not with NAG nor hyaluronidase activities. Fifty-one percent of systemic allergic reactions to IFA stings occurred in summer, and 19% occurred in spring. A reported demographic survey demonstrated a higher incidence of IFA stings in the spring (39.9%) with a lower attack rate in the summer (31.9%). These findings suggest that the rate of systemic reactions to stings of the IFA may be related to seasonal variations in allergenic potency, as measured by PLA and RAST inhibition, rather than the sting attack rate.
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PMID:Seasonal variation in antigens of the imported fire ant Solenopsis invicta. 373 84

The enzyme contents of four venom samples of Calloselasma rhodostoma were analyzed. The venoms contained phosphodiesterase, alkaline phosphomonoesterase, 5'-nucleotidase, protease, phospholipase A, L-amino acid oxidase, hyaluronidase, arginine ester hydrolase, arginine amidase, fibrinogenase and coagulant enzyme activities. There is significant variation in the contents of coagulant enzyme, arginine ester hydrolase, hyaluronidase, protease, phosphodiesterase, alkaline phosphomonoesterase and L-amino acid oxidase. DEAE-Sephacel ion exchange chromatography of the venom resolved it into eight major protein fractions. The eight fractions were heterogeneous and exhibited more than one type of enzymatic activity. The 5'-nucleotidase, alkaline phosphomonoesterase, protease, coagulant enzyme, arginine ester hydrolase, arginine amidase and fibrinogenase exist in multiple forms.
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PMID:Enzymatic activities of Calloselasma rhodostoma (Malayan pit viper) venom. 375 Mar 51

The hemagglutinating factor (hemagglutinin) of Bacteroides gingivalis was prepared from the supernatant of a 5-day diffusate broth culture by ammonium sulfate precipitation and column chromatography with a hydrophobic column of Phenyl-Sepharose CL-4B, DEAE-Sephadex A-50, and Sephadex G-100 gel filtration. The hemagglutinating activity of the preparation was 53.3 times higher than that of ammonium sulfate precipitate. In electron microphotographs, hemagglutinin appears to have a vesicle or tubelike structure. The hemagglutinating activity of intact cells was completely destroyed by heating at 100 degrees C for 10 min, but the activity of extracted hemagglutinin was heat stable. The activity of hemagglutinin was inhibited by L-arginine and L-lysine and partially inhibited by phospholipase D, but it was not affected by proteolytic enzymes, neuraminidase, hyaluronidase, lipase, phospholipase A and C, or sugars. The B. gingivalis hemagglutinin appeared to be comprised mainly of a 40,000-molecular-weight material. The Fab fragment of immunoglobulin G prepared from rabbit antiserum to whole cells of B. gingivalis and monoclonal antibody against the hemagglutinin bound to the cell surface and inhibited the hemagglutinating activity of both the cells and the purified hemagglutinin.
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PMID:Purification and properties of hemagglutinin from culture supernatant of Bacteroides gingivalis. 378 21

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

Between 1979 and 1983 230 patients visited our clinic in connection with allergic reactions after insect stings. One hundred six patients were subjected to a diagnostic provocation test with a live insect; 86 of these patients had a history of systemic reactions and a positive skin test and RAST with insect venom. Thirty-one of these patients, including one patient with a negative RAST and another with a negative skin test, demonstrated a generalized reaction and were subjected to immunotherapy with pure insect venom. Comparison of the diagnostic data from 31 patients with reactions with those of the 57 nonreacting patients from the 86 patients aforementioned reveals that at this time only a provocation test with a live insect can provide the evidence of an allergy to insect venom leading to such a severe generalized reaction that admission to probably lifelong immunotherapy is justified. The measurement of the venom-specific IgG, the ratio of IgG/IgE, and (for bee patients) the serum antibody titer against the bee venom components phospholipase A and hyaluronidase did not improve the diagnosis of a current hypersensitivity against insect venom.
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PMID:The evaluation of the common diagnostic methods of hypersensitivity for bee and yellow jacket venom by means of an in-hospital insect sting. 398 40

(1) Block of conduction and marked increase in permeability of the squid giant axon, when surrounded by adhering small nerve fibers, is caused by the venoms of cottonmouth, ringhals, and cobra snakes and by phospholipase A (PhA). This phenomenon is associated with a marked breakdown of the substructure of the Schwann sheath into masses of cytoplasmic globules. Low concentrations of these agents which render the axons sensitive to curare cause less marked changes in the structure of the sheath. (2) Rattlesnake venom, the direct lytic factor obtained from ringhals venom, and hyaluronidase caused few observable changes in structure, correlating with the inability of these agents to increase permeability. (3) Cottonmouth venom did not alter the structure of giant axons freed of all adhering small nerve fibers. This is in agreement with previous evidence that the venom effects are due to an action of lysophosphatides liberated as a result of PhA action. Cetyltrimethylammonium chloride, a cationic detergent, produces effects that resemble those of venom and PhA. (4) The results provide evidence that PhA is the component of the venoms that is responsible for their effects. It also appears that the Schwann cell and possibly the axonal membrane are the major permeability barriers in the squid giant axon.
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PMID:Fine structural alterations associated with venom action on squid giant nerve fibers. 417 May 46


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