Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.2.1.23 (beta-galactosidase)
14,648 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We previously described the isolation of three identical complementary DNA (cDNA) clones, constructed from Orchard/Cocksfoot grass (Dactylis glomerata) anther messenger RNA (mRNA), expressing a 140,000 MW beta-galactosidase fusion protein recognized by IgE antibodies in atopic sera. Partial nucleotide sequencing and inferred amino acid sequence showed greater than 90% homology with the group II allergen from Lolium perenne (Lol II) indicating they encode the group II equivalent, Dac g II. Western blot immunoprobing of recombinant lysates with rabbit polyclonal, mouse monoclonal and human polyclonal antisera demonstrates immunological identity between recombinant Dac g II, Lol p I and Lol p II. Similar cross-identity is observed with pollen extracts from three other grass species: Festuca rubra, Phleum pratense and Anthoxanthum odoratum. Recombinant Dac g II was recognized by species- and group-cross-reactive human IgE antibodies in 33% (4/12) of sera randomly selected from grass-sensitive individuals and in 67% (14/21) of sera from patients receiving grass pollen immunotherapy, whilst 0/4 sera from patients receiving venom immunotherapy alone contained Dac g II cross-reactive IgE. Cross-reactive IgG4 antibodies were detectable in 95% of sera from grass pollen immunotherapy patients. These preliminary data suggest that conventional grass pollen allergoid desensitization immunotherapy may induce IgE responses to a cross-reactive epitope(s) co-expressed by grass pollen groups I and II (and possibly group III) allergens.
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PMID:Recombinant pollen allergens from Dactylis glomerata: preliminary evidence that human IgE cross-reactivity between Dac g II and Lol p I/II is increased following grass pollen immunotherapy. 152 48

In order to establish a test system for grass pollen allergy based on the use of recombinant allergens we chose timothy grass (Phleum pratense), a widely spread grass, as a model. From a lambda gt11 cDNA expression library that we had constructed from pollen RNA of timothy grass (P. pratense), we had obtained with serum IgE from a grass pollen-allergic individual 60 IgE-binding clones. By differential testing with sera from different grass pollen-allergic patients, we selected three distinct clones encoding Phl p I (group I), Phl p V (group V) and profilin from timothy grass, which when used together allowed the diagnosis of grass pollen allergy in 97 out of 98 tested grass pollen-allergic patients employing a simple plaque lift technique. This recombinant test based on plaque lifts containing allergen-beta-galactosidase fusion proteins was compared with IgE immunoblots using crude pollen protein extracts from timothy grass. Both methods were in good agreement with RAST scores and clinical data, and proofed to be useful for the diagnosis of grass pollen allergy. Our results further indicate that a limited panel of only two recombinant grass pollen allergens, Phl p I and Phl p V, together with the plant panallergen profilin could be sufficient for the diagnosis and possibly immunotherapy of grass pollen allergy.
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PMID:Diagnosis of grass pollen allergy with recombinant timothy grass (Phleum pratense) pollen allergens. 159 49

In this study, recombinant Poa pratensis (Poa p) IX allergens were examined for their in vivo allergenicity and antigenicity. Immunization of mice with a fusion protein (FP) comprising beta-galactosidase and recombinant KBG8.3 (rKBG8.3) allergen induced high titres of both IgG and IgE antibodies. By contrast, immunization with rKBG60.2, which represents the N-terminal fragment of rKBG8.3, induced only IgG antibodies. The IgE antibody titre specific to Kentucky Bluegrass (KBG) was significantly higher than that to beta-galactosidase. Moreover, KBG-specific IgE antibodies showed no apparent decrease in their titres until 60 days after immunization, whereas the beta-galactosidase-specific IgE antibodies disappeared after 40 days. The antibodies induced with rKBG8.3 in mice were capable of inhibiting the binding of human IgE antibodies to KBG pollen allergens, which indicated that rKBG8.3-specific murine antibodies recognized epitopes similar to those recognized by human IgE antibodies. Analysis of allergenic cross-reactivities of rKBG8.3 with components from five other species of grass pollens revealed that IgE antibodies induced by this allergen are capable of binding in vivo to components from other grass pollens. These results suggest that the mouse may serve as a model for the manipulation of IgE responses to recombinant allergens or their chemically modified derivatives.
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PMID:Induction of IgE antibodies in mice with recombinant grass pollen antigens. 162 94

Entamoeba histolytica-specific serum IgG, IgA, IgM and IgE antibodies were assayed in cases of amoebiasis in an endemic area. Patient groups consisted of amoebic liver abscess (n = 18), preabscess hepatic amoebiasis (n = 22) and amoebic colitis (n = 30). Control subjects comprised 26 asymptomatic cyst passers, 13 giardiasis cases, 20 typhoid patients and 24 non-amoebic individuals. Serum IgG was assayed by ELISA, using a monoclonal anti IgG beta-galactosidase (IgG beta-gal) conjugate, a polyclonal avidin biotin horse radish peroxidase (AB-HRP), and a polyclonal anti IgG horse radish peroxidase (IgG HRP) conjugate. IgA and IgM were assayed by the beta-gal ELISA and IgE by AB-HRP. Diagnostically significant IgG and IgA while lower IgM and IgE antibody levels were seen in extraintestinal cases. About 40% of suspected pre-abscess hepatic amoebiasis cases were confirmed by antibody estimation. All isotype levels in most dysentery cases were in the range of the controls.
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PMID:Detection of IgG, IgA, IgM and IgE antibodies in invasive amoebiasis in endemic areas. 169 66

Entamoeba histolytica--specific serum IgG, IgA, IgM and IgE were assayed in cases of amoebiasis in an endemic area. Patient groups consisted of amoebic liver abscess (n = 18), pre abscess hepatic amoebiasis (n = 22) and amoebic colitis (n = 30). Control subjects comprised 26 asymptomatic cyst passers, 13 giardiasis cases, 20 typhoid patients and 24 non amoebic individuals. Serum IgG was assayed by ELISA: using a monoclonal anti IgG beta-galactosidase (IgG beta-gal) conjugate, a polyclonal avidin biotin horse radish peroxidase (AB-HRP) and a polyclonal anti IgG horse radish peroxidase (IgG HRP) conjugate. IgA and IgM were assayed by the beta-gal ELISA and IgE by AB-HRP. Diagnostically significant IgG and IgA while lower IgM and IgE levels were seen in extra intestinal cases. About 40% of suspected pre abscess hepatic amoebiasis cases were confirmed by antibody estimation. All isotype levels in most dysentery cases were in the range of the controls. Inter assay coefficient of variation and assay specificity/sensitivity are also discussed.
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PMID:Detection of IgG, IgA, IgM and IgE in antibodies in invasive amoebiasis in endemic areas. 213 1

Watersoluble antigens of Candida albicans were sequentially extracted from intact and disrupted yeast cells grown on protein-free agar, and analysed on immunoblots after SDS-PAGE. Washing of the cells in saline before proper extraction resulted in loss of 47.2% of the total carbohydrate and 1.5% of the total protein. The protein fraction contained 14 antigenic bands when analysed with hyperimmune rabbit antisera. Four of these bound IgE when probed with a RAST-positive serum pool and beta-galactosidase-labelled anti-IgE. Extraction of the disrupted cells resulted in 15% of the total carbohydrate and 94% of the total protein. The cytoplasmic protein fraction showed 69 antigenic bands, 13 of which bound IgE. The carbohydrate fraction contained mannan, which was found in the washing solutions and in the surface extract as well as in the cytoplasmic extract. Allergens found in washing solutions were also present in cytoplasmic fraction. This study suggests that the rapid release of allergens from saprophytic C. albicans cells on mucous membranes of the body may cause continuous exposure and result in sensitization.
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PMID:Distribution of watersoluble antigens and allergens of Candida albicans in blastospore cell extract fractions. 217 82

Lambda gt11 clones expressing the major house dust mite allergen, Der p II, have been reported to react with IgE in the serum of a high proportion of allergic patients. The clones described, however, only produced small quantities of protein which was not fused to the beta-galactosidase of the vector. A construct of the Der p II is described which produces a fusion of Der p II, minus its leader sequence, with the glutathione-S transferase in the pGEX vector. This could be readily isolated and was shown to react with IgE in 22 of 24 patient sera showing reactivity to native Der p II, the sera not reacting having low reactivity to native protein. Absorption analysis showed that the recombinant material removed most of the IgE reactivity of patients to native Der p II. The construct described, therefore, should be valuable for quantitative studies of a pure mite allergen.
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PMID:Expression of Dermatophagoides pteronyssinus allergen, Der p II, in Escherichia coli and the binding studies with human IgE. 218 17

The allergen composition of crude extract from sap (latex) of the weeping fig (Ficus benjamina) was investigated by sodium dodecyl sulphate-polyacrylamide gel electrophoresis and immunoblotting. The allergenic components were detected by sera from 11 occupationally exposed plant keepers, of whom 7 were non-atopic, and from 9 non-occupationally exposed atopic patients with a positive radio-allergosorbent test to weeping fig. The allergen-antibody complexes were visualized by rabbit anti-IgE and beta-galactosidase-labelled sheep anti-rabbit IgG, using a chromogenic insoluble substrate. A total of 11 allergenic components were identified. Three of them were found to be major allergenic components, identified by more than 50% of the investigated sera. These 3 IgE-binding components had molecular weights of approximately 29,000, 28,000 and 25,000 daltons, respectively. The major allergenic components were denatured by heat in the temperature range of 60-90 degrees C.
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PMID:Characterization of allergenic components in sap extract from the weeping fig (Ficus benjamina). 234 Nov 92

Monoclonal antibodies (MAb) which recognize distinct epitopes on human immunoglobulin E have been used to develop two-site sandwich radio- and enzyme-linked immunoassays for the quantitation of human IgE. In the first step, a purified anti-IgE MAb coated to polyvinyl or polystyrene microtiter plates specifically bound the IgE contained in the samples. In the second step, another anti-IgE MAb (either iodinated or conjugated to beta-galactosidase) directed to a different antigenic determinant was used to estimate the amount of bound IgE. This simple method permitted the determination of IgE concentrations of 10 ng/ml and greater in about 3 h. Coefficients of variation on a single day did not exceed 7.5% for IgE levels, covering a wide range of the standard curve. The values obtained on serum samples showed a good correlation with those obtained using the paper radioimmunosorbent test (PRIST).
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PMID:Quantitative measurement of human immunoglobulin E using monoclonal antibodies to distinct epitopes. 242 16

A Terasaki tray-based ELISA system was developed for the quantitative measurement of antigen-specific and total IgE antibodies in 5 microliter samples of mouse serum dilutions. The assay was based upon non-competitive binding of mouse IgE antibodies between the immobilized appropriate antigen or capture antibodies and the detecting rabbit antibodies. A conjugate of protein A-labelled beta-galactosidase and the fluorigenic substrate methylumbelliferyl-beta-D-galactoside were used as a detecting system. The resulted fluorescence could be measured rapidly and automatically using an inverted micro-fluorimeter. These measurements were automatically transformed into absolute concentrations by a microprocessor-based program using a four-parameter logistic function and an absolute IgE standard. The assay was shown to have a detection limit of 0.04 ng/ml and a range of linearity of 0.04-20 ng/ml, which is sufficient to measure IgE concentrations in mouse serum.
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PMID:Terasaki-ELISA for murine IgE antibodies. II. Quantitation of absolute concentration of antigen-specific and total IgE. 249 54


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