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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Industrial and engineering chemistry 9 (1937), S. 201-202 
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Clinical & experimental allergy 23 (1993), S. 0 
    ISSN: 1365-2222
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Total RNA was extracted from the whole body of American cockroach Periplaneta americana) using chaotropic salt guanidine isothiocyanate in the presence of 2-mercaptoethanol (2-ME). Polyadenylated mRNA was isolated by oligothymidylic acidcellulose chromatography and mRNA was translated using a rabbit reticulocyte lysate system. The translation, as judged by the incorporation of-S-tnethionine, was obtained with poly(A)‘*’RNA, where an approximately 9-5-fold increase in label incorporation over control was achieved. Analysis of translation products by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) in combination with autoradiography showed that many proteins with apparent molecular weights ranging from 12 to 200 kD were synthesized, and no labelled proteins were found with negative RNA control and poly(A) RNA. Immunoprecipitation studies performed using polyclonal and monoclonal antibodies revealed that synthesized proteins of MW 90, 78, 72, 49, 45, and 26 kD corresponded with previously identified principal and major allergens of American cockroach from our laboratory. In addition, the allergenicity of the translation mixtures was also confirmed by fluoroallergosorbent test (FAST) inhibition studies with IgE antibodies of human reaginic serum pool.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Science Ltd
    Clinical & experimental allergy 35 (2005), S. 0 
    ISSN: 1365-2222
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Background Histo-blood groups, ABO, Lewis (Le) and secretor (Se) were found to be associated with lower lung function and wheezing in coal miners as well as in asthmatic children in some studies but not others, possibly reflecting the genetic heterogeneity among different ethnicities and local environmental exposure.Objective The present study was conducted to determine the association between ABO, Lewis and secretor genetic complex with susceptibility of childhood asthma in Taiwan.Methods We randomly selected 136 asthmatic children and 161 age-matched controls from a childhood asthma survey conducted in primary schools. ABO and Lewis blood groups were determined by red blood cell agglutination methods. Analysis of Se genotype was performed by PCR with sequence-specific primers.Results There was a higher prevalence rate in secretor subjects (Se/Se) (odds ratio (OR)=1.7, confidence interval (CI)=1.022–2.938) in asthma as compared with controls. The combined effect of these three blood systems revealed that blood group O/secretor phenotype (Se/Se) (OR=2.7, CI=1.126–6.033), and blood group O/Le(a−b−) (OR=3.6, CI=1.080–11.963, P〈0.03) individuals were significantly associated with asthma. The Lewis Le(a−b−) recessive genotype (OR=3.3, CI=1.267–8.482), or the joint blood group O/Le(a−b−) phenotype (OR=5.2, CI=1.259–21.429, P〈0.02), was significantly associated with high serum IgE (〉500 IU), respectively. There was no association of these three blood systems with the sensitivity of dust mite, Dermatophagoide pteronyssinus, in our study population.Conclusions We concluded that blood group O/secretors (Se/Se) and O/Le(a−b−) were associated with childhood asthma, and may act as one of the predominant factors for environmental triggers of allergy for asthmatic children in Taiwan.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Industrial and engineering chemistry 9 (1937), S. 533-534 
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    The @journal of physical chemistry 〈Washington, DC〉 62 (1958), S. 877-878 
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Industrial and engineering chemistry 2 (1930), S. 405-407 
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Industrial and engineering chemistry 4 (1932), S. 264-265 
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
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  • 8
    ISSN: 0044-8486
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Type of Medium: Electronic Resource
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  • 9
    ISSN: 1398-9995
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Background:  Forcipomyia taiwana is a tiny, blood-sucking midge that cause intense pruritis and swelling in sensitive individuals. It is distributed island-wide in rural Taiwan and Southern China.Objective:  This study aimed to study the allergic immune responses and identify F. taiwana allergens.Methods:  Crude whole body F. taiwana extracts were prepared with phosphate-buffered saline. The specific IgE antibody was determined by enzyme-linked immunoassay and immunoblotting. Protein was analyzed by electrospray ionization tandem mass spectrometry.Results:  Among the 372 subjects that were exposed to F. taiwana bites, 179 (48%) reported an immediate skin reaction with/without delay reaction and 41(11.1%) reported a solely delay reaction. The skin of 21 subjects was tested with F. taiwana extract. Of these 21 subjects, 12 (57.1%) produced immediate skin reactions and contained high levels of specific IgE antibody against F. taiwana. Immunoblotting revealed that 11 allergenic components are able to bind specific IgE. Allergens of 22, 24, 35, 36, and 64 kDa bound 50, 50, 75, 66.7, and 75% of IgE-containing sera tested, respectively. Tryptic fragments of the 24, 35, 36, and 64 kDa allergens were analyzed by ESI-MS/MS. Selected tryptic peptides of 24, 35, and 36, and 64 kDa allergens exhibited significant sequence identity with triosephosphate isomerase of Anopheles merus,Tenebrio molitor,Ochlerotatus togoi, and Chrysops vittatus, fructose 1,6-bisphosphate aldolase of Antheraea yamamai and Homalodisca coagulata, and a slow muscle myosin S1 heavy chain of Homarusamericanus and a protein with unknown function from A. gambiae, respectively. The 35 and 36 kDa proteins may represent different isoforms of the fructose 1,6-bisphosphate aldolase.Conclusion:  We conclude that immediate reaction to F. taiwana bites is IgE mediated and the 24 (For t 1), 35 (For t 2), and 64 kDa (For t 3) proteins are candidates for major F. taiwana allergens. Further studies are needed to confirm these allergens.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Oxford, UK : Munksgaard International Publishers
    Allergy 58 (2003), S. 0 
    ISSN: 1398-9995
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Background: The Per a 3 is a species-specific allergen of the American cockroach (Periplaneta americana) related to insect hemolymph proteins and includes four known isoallergens. This study aimed to identify Per a 3 linear IgE-binding epitopes.Methods: Per a 3 recombinant fragments were generated from the recombinant Per a 3.01 allergen (685 amino acid residues) by using existing restriction sites or by using polymerase chain reaction products, and expressed in Escherichia coli. Antigenicities were assessed by immunoblotting, enzyme-linked immunosorbent assay (ELISA), and binding inhibition with human IgE.Results: Human IgE recognized recombinant fragments 340–425, 466–579, 502–595, and 595–636 as revealed by immunoblotting and ELISA. On the other hand, the N-terminal fragment 1–399, recombinants 410–443, 472–551, 502–579, 606–636, and the C-terminal fragment 636–685 were unable to bind human IgE. Amino acid sequences 400–409, 466–471, 580–595, and 595–605 were shown to be required for IgE binding to the Per a 3.01 allergen, suggesting that the C-terminus contains most of the IgE-binding sites. Four peptides corresponding to these IgE-binding amino acid sequences were synthesized. These peptides reacted with most sera (62.5–87.5%) tested as revealed by ELISA, demonstrating a heterogeneous IgE-binding response. Moreover, preincubation of IgE-positive recombinant proteins and synthetic peptides with atopic IgE resulted in marked inhibition of the IgE binding to Per a 3.01 allergen. Amino acid sequences 400TVLRDPVFYQ409, 466NNVDQI471, 580VDKGHNYCGYPENLLI595, and 595IPKGKKGGQAY605 of the major recombinant American cockroach Per a 3.01 allergen were involved in IgE binding.Conclusion: These findings will advance our understanding of the antigenic structures responsible for allergenicity to the American cockroach, thereby providing strategies for the development of immunotherapies.
    Type of Medium: Electronic Resource
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