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  • 1
    Electronic Resource
    Electronic Resource
    Synthesis and pharmacological evaluation of a series of analogs of 1-methylisoguanosine (1981)
    s.l. : American Chemical Society
    Journal of medicinal chemistry 24 (1981), S. 947-954 
    Details
    ISSN: 1520-4804
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/jm00140a007
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  • 2
    Electronic Resource
    Electronic Resource
    Structure-Activity Studies on Drug-Induced Anaphylactic Reactions (1994)
    s.l. : American Chemical Society
    Chemical research in toxicology 7 (1994), S. 703-721 
    Details
    ISSN: 1520-5010
    Source: ACS Legacy Archives
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/tx00042a001
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Activation of a subpopulation of orexin/hypocretin-containing hypothalamic neurons by GABAA receptor-mediated inhibition of the nucleus accumbens shell, but not by exposure to a novel environment (2004)
    Oxford, UK : Blackwell Science Ltd
    European journal of neuroscience 19 (2004), S. 0 
    Details
    ISSN: 1460-9568
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: γ-Amino butyric acid (GABA)A receptor stimulation in the nucleus accumbens shell produces intense hyperphagia in rats and increases Fos expression in the lateral hypothalamus. To explore the involvement of hypothalamic orexin/hypocretin- or melanin concentrating hormone-immunoreactive neurons in this effect, the GABAA agonist, muscimol (0, 50 ng), was infused directly into the nucleus accumbens shell of rats; 90 min later, their brains were collected and subsequently processed for immunohistochemistry. A group exposed to a novel environment was included to evaluate the specificity of Fos expression changes with regard to general arousal. Alternating sections through the hypothalamus were double-stained for orexin/hypocretin–Fos or melanin concentrating hormone–Fos combinations. Intra-accumbens shell muscimol treatment significantly increased the percentage of orexin/hypocretin-containing neurons expressing Fos in the lateral, but not medial, portion of the perifornical/lateral hypothalamic area. Regardless of treatment condition, greater percentages of orexin/hypocretin-containing neurons in the medial portion of the hypothalamus expressed Fos relative to cells located more laterally. None of the manipulations increased Fos expression in melanin concentrating hormone-immunoreactive neurons. Muscimol treatment also markedly increased Fos expression in the arcuate nucleus, which connects reciprocally to the lateral/perifornical hypothalamic area. Thus, orexin/hypocretin-containing neurons in lateral sectors of the hypothalamus, along with cells in the arcuate nucleus, display phasic increases in Fos expression after an orexigenic pharmacological manipulation of the nucleus accumbens shell, but to a lesser degree after the heightened arousal associated with exposure to a novel environment.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1460-9568.2004.03093.x
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  • 4
    Electronic Resource
    Electronic Resource
    The specificity of the binding of platelet activating factor (PAF) to anti-PAF antibodies (1990)
    Chicester [u.a.] : Wiley-Blackwell
    Journal of Molecular Recognition 3 (1990), S. 169-173 
    Details
    ISSN: 0952-3499
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Quantitative hapten inhibition experiments employing sheep anti-PAF antibodies and selected PAF analogues were undertaken with the aim of defining the antigenic determinant structures complementary to the antibody combining sites. The most important fine structural features for inhibition of antibody binding to PAF were shown to be an acetyl group at position 2 of the phospholipid glycerol backbone and an ether group at position 1. Of the naturally occurring compounds, C16- and C18:1-PAF proved to be the most potent inhibitors and more active than C18-PAF while phospholipids with a propionyl, butyryl or hexanoyl group at position 2 showed either weak or no inhibitory activity. The 1-acyl, thioether and deoxy analogues proved inactive. Variations in the polar head group of PAF were found to be less critical with, for example, the dimethyl and ethanolamine derivatives retaining some activity. This antibody recognition pattern is very similar to that of the PAF receptor, although the antibodies appear to have a more specific requirement for an acyl linkage at position 2.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jmr.300030406
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  • 5
    Electronic Resource
    Electronic Resource
    β-Lactam drug allergens: Fine structural recognition patterns of cephalosporin-reactive IgE antibodies (1996)
    Chicester [u.a.] : Wiley-Blackwell
    Journal of Molecular Recognition 9 (1996), S. 287-296 
    Details
    ISSN: 0952-3499
    Keywords: cephalosporin allergens ; cefaclor ; β-lactam allergy ; drug allergy ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Lack of experimental findings on the spectrum of cephalosporin allergenic determinants has hindered diagnosis of adverse reactions to these drugs and retarded understanding of allergenic cross-reactions between cephalosporins and between cephalosporins and penicillins. Subjects allergic to the widely used cephalosporin antibiotic cefaclor have serum immuno globulin (Ig) E antibodies that react with the drug. Quantitative hapten inhibition studies employing sera from subjects allergic to cefaclor revealed fine structual recognition differences between the combining site specificities of cefaclor-reactive IgE antibodies in the sera of different subjects. Unlike penicillins, where discrete side chain or thiazolidine ring determinants alone may be recognized, IgE binding determinants on cefaclor encompassed the entire molecule. Fine structural recognition specificity differences at positions R1 (side-chain) and R2 (substituent attached to dihydrothiazine ring) were detected between IgE antibodies in different sera. Some antibodies showed clear preferential recognition of the aminobenzyl group at position R1 and Cl at R2 while with others, a greater degree of recognition tolerance was seen at R1 where, for example, the aminohydroxybenzyl or aminodihydrobenzyl groups were recognized, and at R2 where a methyl or even an ester group was tolerated. As with the penicillins, cephalosporins as allergens cannot simply be considered as a group of compounds with a common allergenic determinant structure. IgE antibodies that bind to cefaclor show great heterogeneity indicated by clear, fine structural differences in recognition of the R1 and R2 groups on the drug.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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    Paper (German National Licenses)
  • 6
    Electronic Resource
    Electronic Resource
    Editorial (1993)
    Weinheim : Wiley-Blackwell
    Electrophoresis 14 (1993), S. 829-830 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.11501401132
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  • 7
    Electronic Resource
    Electronic Resource
    Intra-species cross-reactivity of house dust mite allergens separated by protein blotting and detected by selective elution of mite components and IgE antibodies (1993)
    Weinheim : Wiley-Blackwell
    Electrophoresis 14 (1993), S. 923-925 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: A complex and varied antibody response to allergens, in particular Dermatophagoides pteronyssinus, is observed in the serum of allergic patients. To examine the role of cross-reacting antigenic determinants in allergy, a strategy has been devised for isolating antibody populations that bind to individual polypeptides of an allergen source separated by sodium dodecyl sulfate-polyacrylamide electrophoresis and electroblotted to nitrocellulose. Polypeptides are identified on the blots, desorbed and coupled to CNBr-activated paper discs. The coupled discs are then used as immunoadsorbent surfaces for the binding of antibodies from allergic sera. Antibodies eluted from the polypeptide immunoadsorbents are then used to reprobe protein blots of the allergen. Results are presented which demonstrate strong cross-reaction between two major mite allergens, Der p I and Der p III, and some weaker intra-species cross-reactivities.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.11501401147
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  • 8
    Electronic Resource
    Electronic Resource
    Comparison of semi-dry and conventional tank-buffer electrotransfer of proteins from polyacrylamide gels to nitrocellulose membranes (1987)
    Weinheim : Wiley-Blackwell
    Electrophoresis 8 (1987), S. 384-387 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The rate of transfer of radiolabelled proteins from sodium dodecyl sulphate-polyacrylamide gels to nitrocellulose membranes by semi-dry blotting and electro-transfer in a tank of buffer with and without sodium, dodecyl sulphate was quantitated. The semi-dry blot method transferred about two thirds of most proteins in the first hour; less than one tenth of the total protein in the gel was transferred in the following hour. Conventional transfer in a tank of buffer without sodium dodecyl sulphate was dependent on the molecular weight and isoelectric point of the proteins. The efficient migration of high molecular weight and basic proteins required the presence of sodium dodecyl sulphate. The efficiency of transfer to the nitrocellulose depended both on the transfer method and on the pore size of the nitrocellulose. Almost all protein which left the gel could be accounted for when 0.1 μm pore size was used, but when 0.45 μm pore size was used in combination with semi-dry blotting or transfer in a tank of buffer containing 0.1 % sodium dodecyl sulphate, less than 60 % of the protein could be accounted for after transfer. When transfers by two of the methods were compared using a mite extract as an antigen source and a group of miteallergic sera for detection, the same proteins were detected in each case but those which had been transferred by the semi-dry blot method were more easily detected by the antisera used.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150080904
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  • 9
    Electronic Resource
    Electronic Resource
    Characterisation of allergens by protein blotting (1987)
    Weinheim : Wiley-Blackwell
    Electrophoresis 8 (1987), S. 452-463 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Techniques developed for protein blotting have been applied to the characterisation of allergen extracts. Such extracts, used for the diagnosis and therapy of allergic diseases, are highly variable in their content of active components. Protein blotting allows the direct identification of those components in an extract which bind human immunoglobulin E and cause allergic symptoms. It also allows the components to be defined in terms of molecular weight, isoelectric point and the frequency and intensity of IgE-binding by individual allergens. Because of the large number of samples which can be handled in a single experiment, protein blotting of allergens allows the identification of the individual allergen recognition spectra of large numbers of allergic patients. The resolution of components, loss of antigenicity, and aspects of blocking and probing which are important in identifying IgE-binding components are reviewed. A table of allergen sources investigated by protein blotting is included and important sources of allergens, such as pollens, mites and fungi are discussed in detail.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150080915
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  • 10
    Electronic Resource
    Electronic Resource
    Immunoaffinity analysis of cross-reacting allergens by protein blotting (1993)
    Weinheim : Wiley-Blackwell
    Electrophoresis 14 (1993), S. 917-922 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: IgE antibodies from sera having reactivity against ryegrass pollen protein allergens, wheat endosperm protein allergens and also several other cereal protein allergens were adsorbed with either ryegrass pollen or the wheat/globulin fraction immobilised on solid phases and subsequently eluted with low pH buffer. The eluted antibodies were reacted with sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) blots of the different allergens. Antibodies adsorbed and subsequently eluted from the two allergen sources recognised different spectra of proteins in the ryegrass pollen and cereal allergen sources and indicated the degree of immunological cross-reactivity. Intra-species cross-reactivity of IgE antibodies was demonstrated employing similar methods to those used for the pollen and cereal allergens by using a recombinant allergen from the venom of the ant Myrmecia pilosula as the immunoadsorbant protein on the solid phase.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.11501401146
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