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  • 1
    Electronic Resource
    Electronic Resource
    Group V allergens in grass pollens: IV. Similarities in amino acid compositions and NH2-terminal sequences of the Group V allergens from Lolium perenne, Poa pratensis and Dactylis glomerata (1992)
    Oxford, UK : Blackwell Publishing Ltd
    Clinical & experimental allergy 22 (1992), S. 0 
    Details
    ISSN: 1365-2222
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Monoclonal antibodies (PpV4) raised against Phleum pratense group V allergen were used for immuno-affinity chromatography of cross-reacting group V allergens from related grass species. Fractions enriched in group V allergen were obtained from Lolium perenne, Poa pratense and Dactylis glomerata extracts. The major components in these fractions were found in the Mwr range 25–28 kD. IgE binding to these components was shown using a pool of grass allergic sera, by SDS-PAGE immunoblotting. These fractions were electroblotted from tricine SDS-PAGE gels onto a polyvinylidenedifluoride membrane and selected group V bands were directly cut out and used for amino acid analysis and NH2-terminal sequencing.Both the amino acid compositions and the NH2-terminal sequences obtained for each group V allergen were almost similar to each other and to the sequence and composition of the previously described allergen Phl p V from Phleum pratense. A common trait of the investigated allergens, is the very high contents of alanine (25–32%) and the presence of the modified amino acid, hydroxyproline.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2222.1992.tb00152.x
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  • 2
    Electronic Resource
    Electronic Resource
    HLA-DR and HLA-DP genotypes and immunoglobulin E responses to common major allergens (1994)
    Oxford, UK : Blackwell Publishing Ltd
    Clinical & experimental allergy 24 (1994), S. 0 
    Details
    ISSN: 1365-2222
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract. In order to test for human histocompatibility leucocyte antigens (HLA) class II restriction of IgE responses, 431 subjects from 83 families were genotyped at the HLA-DR and HLA-DP loci and serotyped for IgE responses to six major allergens from common aero-allergen sources. A possible excess of HLA-DR 1 was found in subjects who were responsive to FeldI compared with those who were not (Odds Ratio (OR) = 2, P = 0.002), and a possible excess of HLA-DR4 was found in subjects responsive to Alt a I (OR = 1–9, P = 0.006). Increased sharing of HLA-DR/DP haplotypes was seen in sibling pairs responding to both allergens. Der p I, Der p II, Phi p V and Can f I were not associated with any definite excess of HLA-DR alleles. No significant correlations were seen with HLA-DP genotype and reactivity to any of the allergens. The results suggest class II HLA restriction is insufficient to account for individual differences in reactivity to common allergens.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2222.1994.tb00931.x
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  • 3
    Electronic Resource
    Electronic Resource
    Predominance of the major allergen (Alt a I) in Alternaria sensitized patients (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Clinical & experimental allergy 23 (1993), S. 0 
    Details
    ISSN: 1365-2222
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Thirty-nine patients sensitized to Alternaria were evaluated using titrated skin-prick test (SPT), histamine release studies (HR), inhibition of RAST and immunoblotting studies. To determine the relevance of the major allergen, Alt a I, specific rabbit antibodies against Alt a I and Alt a B were used. The antibodies were preincubated at different concentrations: (i) with the Alternaria allergen dose required for maximum response in the HR assay (10 BU/ml) and (ii) with the Alternaria antigen coupled to RAST paper discs (1000 BU/disc). Dose dependent inhibition of histamine release (n= 30, x̄= 80%± 4%, IC30 = 0.69 μg/ml) and of RAST (n= 7, IC30 = 4.4 μg/ml) was found in all patients sensitized to Alternaria as indicated by allergen induced HR. The greater the response to Alternaria in HR, the higher the antibody concentrations necessary for inhibition (P〈0.05). Immunoblot experiments (n=25) using SDS-PAGE showed in all cases IgE- and IgG binding at approximately 28 kD, which is the size reported for the major allergen. All a I. In two cases, slight IgE binding at 45 and 66 kD was also found, while in two other patients, only IgE binding at 66 kD was seen. Our findings emphasize the major importance of Alt a I in patients sensitized to Alternaria.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2222.1993.tb00884.x
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  • 4
    Electronic Resource
    Electronic Resource
    Group V allergens in grass pollens. I. Purification and characterization of the group V allergen from Phleum pratense pollen, Phl p V (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: An allergen from Phleum pratense (timothy) pollen. Phl p V, has been isolated by a combination of copper chelate affinity chromatography and ion exchange chromato-graphy. Phl p V binds IgE from serum of grass-sensitized donors as revealed in immunoelectrophoretic techniques and in SDS PAGE immunoblot, and luminescence immunoassay (LIA) inhibition experiments indicate that the allergen represents a significant part of the IgE binding capacity of the extract. In immunoelectrophoresis, Phl p V is revealed as a single precipitate. However, molecular weight studies show that Phl p V consists of at least two isoforms with similar immunochemical properties, but with different molecular size. After SDS-PAGE treatment purified Phl p V is identified as two IgE-binding components. Phl p Va and Phl p Vb, with molecular weights 33 and 29 kD. After HPLC gel filtration, Phl p Va and Phl p Vb are identified in the major 30-kD eluate. After Sephadex G75 gel filtration of whole pollen extract, Phl p V is identified in fractions corresponding to molecular weights 47 and 25 kD. The 47-kD fraction corresponds to Phl p Va/Phl p Vb as seen in SDS-PAGE, while the 25-kD component presumably corresponds to a degradation product present in whole pollen extract. The NH2-terminal sequence of Phl p V, corresponding to approximately 10% of the molecule, has been determined. The sequence shows minor variations in some residues and contains besides many alanine residues also hydroxyproline; the sequence reveals no homologies to any known NH2 terminal sequence of other proteins. The ammo acid composition, revealing 26 mote % alanine and no cysteine, does not show any similarities to other known amino acid compositions of allergens. From the amino acid composition determination and an immunoelectrophoretic comparison. Phl p V is estimated to represent 6% (w/w) of the whole pollen extract.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2222.1991.tb01661.x
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  • 5
    Electronic Resource
    Electronic Resource
    Group V allergens in grass pollens. II. Investigation of group V allergens in pollens from 10 grasses (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: In an earlier study an allergen from Phleum pratense (timothy) pollen. Phl p V. has been isolated and physicochemically characterized. In this study Phl p V and immunochemically simitar components from other grass pollens (group V allergens) have been investigated using immunoelectrophoretic techniques. To study the allergenic importance of the group V allergens, the allergenic compositions of 10 grass pollen extracts were investigated in crossed radioimmunoelectrophoresis (CRIE) using 20 sera from grass pollen-allergic donors. Group V allergens were identified using monospecific rabbit antibodies raised against Phl p V, anti-phl p V, which react with other group V allergens usually producing dense precipitates in immunoelectrophoresis. In this way group V allergens were identified in eight extracts, and when present the precipitate corresponding to the group V allergen was the dominant IgE binding precipitate. All identified group V allergens bound IgE in at least 17 of the 20 investigated sera. Monospecific rabbit antibodies raised against the group I allergen of Lolium perenne (rye grass), anit-Lol p I. do not precipitate group V allergens, indicating that there are no immunochemical similarities between group I and group V allergens. In SDS-PAGE anti-Phl p V identifies IgE-binding components with molecular weights between 26 and 33 kD. In contrast, anti-Lol p I binds to components of slightly higher molecular weight. Apparently, the group V components are allergens that are physicochemically and immunochemically distinct from group I allergens.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2222.1991.tb01662.x
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  • 6
    Electronic Resource
    Electronic Resource
    On an anomalous individual ofPolistes versicolor (Olivier, 1791) (Vespidae, Polybiinae) (1980)
    Springer
    Insectes sociaux 27 (1980), S. 343-344 
    Details
    ISSN: 1420-9098
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Description / Table of Contents: Resume Nous décrivons, dans cette note, un individu femellé dePolistes versicolor (Olivier, 1791), porteur de deux paires de pattes et de beaucoup d'autres anomalies.
    Notes: Summary An anomalous female ofPolistes versicolor is described. It had only 4 legs and presented many other abnormalities.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02223726
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