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  • 1
    Electronic Resource
    Electronic Resource
    The 40-kilodalton allergen of Candida albicans is an alcohol dehydrogenase: molecular cloning and immunological analysis using monoclonal antibodies (1991)
    Oxford, UK : Blackwell Publishing Ltd
    Clinical & experimental allergy 21 (1991), S. 0 
    Details
    ISSN: 1365-2222
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: To characterize the 40-kilodalton (kD) major allergen of Candida albicans (C. albicans), six monoclonal antibodies (MoAbs) against this allergen were generated. In SDS-polyacrylamide gel electrophoresis and immunoblot analysis, these MoAbs showed four different reaction patterns to antigens of six different Candida species. With the exception of one MoAb, other MoAbs were resistant to periodate treatment indicating non-carbohydrate epitopes were probably being recognized by these MoAbs. These MoAbs were used in the molecular cloning and immunological analysis of the gene coding for the 40-kD allergen. Nucleotide sequence determination of the two λgtl 1 cDNA clones obtained showed that the 40-kD allergen is an alcohol dehydrogenase (ADH) which shares a 70% amino acid sequence homology with the ADH isozyme I of Saccharomyces cerevisiae. This finding was confirmed by positive immunological response of the lysates of the clones obtained and a preparation of ADH of Saccharomyces cerevisiae to various MoAbs and to IgE antibodies in sera of allergic patients.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2222.1991.tb03195.x
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  • 2
    Electronic Resource
    Electronic Resource
    Allergenic components of Candida albicans identified by immunoblot analysis (1989)
    Oxford, UK : Blackwell Publishing Ltd
    Clinical & experimental allergy 19 (1989), S. 0 
    Details
    ISSN: 1365-2222
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Allergenic components of Candida albicans fractionated by SDS–polyacrylamide gel electrophoresis (PAGE) and transferred to nitrocellulose membranes were identified using sera from 30 asthmatic patients who showed positive skin test and RAST (radio-allergosorbent test) to C. albicans. The IgE-binding yeast components in the complex antigen preparation were then detected by reaction with enzyme-labelled anti-human IgE antibodies. They were confirmed by Coomassie blue R-250 staining of the membrane to visualize all protein bands after reaction with the enzyme substrate. The IgE-binding patterns of the sera tested were heterogeneous, displaying a total of 16 identifiable components with molecular weights ranging from 20 to 94 kD. A 40 kD component showed the highest IgE-binding frequency, being recognized by 23 (77%) of the 30 sera examined. The other 15 allergenic components identified were recognized by less than 25% of the sera tested. Only two of the 30 serum samples contained IgE antibodies reactive with seven to eight allergenic components. Ten of the 30 sera reacted with only one allergenic component, and the remaining serum samples recognized two to five of the 16 identified allergens. Results described in this study are applicable to allergen standardization work and provide a basis for further study on the role of C. albicans in clinical allergy.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2222.1989.tb02363.x
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  • 3
    Electronic Resource
    Electronic Resource
    Identification of allergens and antigens of Bermuda grass (Cynodon dactylon) pollen by immunoblot analysis (1988)
    Oxford, UK : Blackwell Publishing Ltd
    Clinical & experimental allergy 18 (1988), S. 0 
    Details
    ISSN: 1365-2222
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Allergens and antigens of Bermuda grass pollen fractionated by SDS-polyacrylamide gel electrophoresis and transferred to nitrocellulose membranes were identified using twenty-one sera of Bermuda grass pollen-allergic patients. The IgE- and IgG-binding pollen components transferred to nitrocellulose were detected by reaction with enzyme-labelled anti-human IgE and anti-human IgG, respectively. There was heterogeneity in both IgE- and IgG-binding patterns of the allergic sera tested. Fourteen pollen components, ranging in molecular weight from 16000 to 88000 daltons, bound to IgE antibodies. Only two of the fourteen allergens identified reacted with IgE antibodies of more than 50% of the twenty-one allergic sera. The pollen component with a molecular weight of 32000 daltons showed by far the highest frequency of IgE binding, being recognized by sixteen (76%) of the twenty-one sera examined. Fifteen (71 %) of the twenty-one sera tested had IgE antibodies that reacted with more than one of the fourteen allergenic components identified. Pollen components recognized by IgE antibodies also reacted with IgG antibodies, and there were components only recognized by IgG antibodies. Results obtained from this study should be useful both clinically and in research.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2222.1988.tb02888.x
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  • 4
    Electronic Resource
    Electronic Resource
    Indoor airbornePenicillium species in Taiwan (1993)
    Springer
    Current microbiology 26 (1993), S. 137-140 
    Details
    ISSN: 1432-0991
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Penicillium species, well-known indoor airborne fungi, are considered to be important causative agents of extrinsic bronchial asthma. For selecting the proper species for clinical investigations, it is important to know which are found indoors. In the present study, 176 plates of modified Mehrlich's Medium were exposed for 20 min in living rooms and bedrooms of 88 homes in Taipei, Taiwan. A total of 5897 colonies of fungi were isolated, varying from one to 329 per house. Of the total, 910 colonies (15.4%) were identified asPenicillium spp. The three most frequently encountered species wereP. citrinum, P. crustosum andP. implicatum. Penicillium citrinum accounted for 40.5% (369 from 28 houses);P. implicatum, for 5.2% (47 from three houses); andP. crustosum, for 2.1% (19 from seven houses).Penicillium citrinum was judged to be the most prevalent airborne fungus in Taiwan. The allergenic significance of this mold is under further investigation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01577367
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  • 5
    Electronic Resource
    Electronic Resource
    Immunoblot analysis of components of barley recognized by IgE antibodies in sera from pig farm workers (1998)
    Weinheim : Wiley-Blackwell
    Electrophoresis 19 (1998), S. 1317-1318 
    Details
    ISSN: 0173-0835
    Keywords: Immunoblotting ; Occupational disorders ; Respiratory disorders ; Barley ; Allergens ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Components of the crude extract of barley, recognized by IgE antibodies in sera from 132 pig farm-workers in southern Taiwan, were investigated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and immunoblotting. Among the sera tested, 43 (32.6%) showed IgE reactivity to 15 components of barley with molecular mass ranging from 148000 to 14000 daltons (Da). Heterogeneity in the IgE-binding patterns of the samples tested was observed. However, the major antigen appears to be the component with about 37 kDa, in 32 (74.4%) of the 43 immunoblot-positive serum samples. Furthermore, components with about 55 and 67 kDa which reacted with 26 (60.5%) and 18 (41.9%) of the positive samples, respectively. These might also be considered as important allergens of the flour made from entire seeds of barley. The results suggest that barley may be considered to play a role in the IgE-mediated occupational respiratory disorders and the 37 kDa component has also been shown to be the major allergen.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150190818
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  • 6
    Electronic Resource
    Electronic Resource
    An improved scheme for the identification of antigens recognized by specific antibodies in two-dimensional gel electrophoresis and immunoblotting (1990)
    Weinheim : Wiley-Blackwell
    Electrophoresis 11 (1990), S. 878-882 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: This paper describes an improved scheme for the identification of antigens in crude extracts recognized by specific antibodies when analyzed by a combination of two-dimensional gel electrophoresis and immunoblotting. First, protein components in gels are electrophoretically transferred to a polyvinylidene difluoride membrane which does not shrink or change dimensions in organic solvents. The efficiency of transfer and the localization of sample proteins on the membrane are checked and recorded by staining the blotting membrane with Fast Green FCF and recording the profile on a transparency. After blocking and the immunoassay, the results are recorded by photography. The sites of immune reaction are marked and the same membrane is restained briefly with Coomassie Brilliant Blue R-250 for the protein profile. Thus antigens in complex mixtures, recognized by antibodies of interest, can easily be identified from the restained membrane. If the whole protein profile is not well demonstrated, when used in combination with the profile recorded on the transparency, spots appearing on the restained membrane can still be used as useful landmarks in the final unequivocal antigenic identification. This improved scheme circumvents problems arising from membrane shrinkage and difficulties in accurately matching immunoreactive spots by conventional procedures and thus provides an accurate, simple and fast approach in the identification of antigens after immunoblotting.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150111018
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