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  • 1
    Electronic Resource
    Electronic Resource
    Persistent photoconductivity in SiGe/Si quantum wells (1998)
    [S.l.] : American Institute of Physics (AIP)
    Journal of Applied Physics 84 (1998), S. 877-880 
    Details
    ISSN: 1089-7550
    Source: AIP Digital Archive
    Topics: Physics
    Notes: Persistent photoconductivity (PPC) has been observed in boron-doped Si1−xGex/Si quantum wells. The decay kinetics of the PPC effect can be well described by a stretched-exponential function, Ippc(t)=Ippc(0)exp[−(t/τ)β](0〈β〈1), which is usually observed in many disorder materials. Through the studies of the PPC effect under various conditions, such as different temperature, different photon energy of photoexcitation, and different Ge content, we identify that the alloy potential fluctuations induced by compositional disorder are the origin of the PPC effect in Si1−xGex/Si quantum wells. © 1998 American Institute of Physics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.368150
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  • 2
    Electronic Resource
    Electronic Resource
    Positive and negative persistent photoconductivities in semimetallic AlxGa1−xSb/InAs quantum wells (1999)
    [S.l.] : American Institute of Physics (AIP)
    Journal of Applied Physics 86 (1999), S. 3152-3158 
    Details
    ISSN: 1089-7550
    Source: AIP Digital Archive
    Topics: Physics
    Notes: We report a detailed investigation of the "positive" persistent photoconductivity (PPC) and "negative" persistent photoconductivity (NPPC) in semimetallic AlxGa1−xSb/InAs quantum wells. The studies of the NPPC and PPC effects have been performed under various conditions, such as different photon energy of excitation, different temperature, different Al composition x, and different well width. It is found that all the previously proposed mechanisms fail to explain several of our observations. We suggest that the NPPC and PPC effects are produced principally by two competing processes. At a high temperature, the photoconduction is dominated by the photogenerated electrons in the InAs well, in which the relaxation of the excess electrons is prohibited by an energy barrier due to the trapping of photoexcited holes by deep defects in the InAs well. As a result, the PPC is observed. At low temperature, electrons in the InAs layer are photoexcited into the local potential minima induced by compositional fluctuations at the AlGaSb and InAs interface, the number of electrons in the InAs well decreases, thus the NPPC occurs. © 1999 American Institute of Physics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.371182
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  • 3
    Electronic Resource
    Electronic Resource
    Changes in the levels of house dust mite specific IgG4 during immunotherapy in asthmatic children (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: Serum levels of IgG subclass and house dust mite (Dermatophagoides pteronyssinus, Dpt) specific IgG4 were evaluated during immunotherapy in asthmatic children. Asthmatic children undergoing long-term immunotherapy (more than 2 years) posed a mean value of total serum IgG4 or Dpt-specific IgG4 antibodies significantly higher than that of patients prior to receiving immunotherapy, asthmatic (placebo) controls, or patients undergoing short-term immunotherapy (less than 1 year) (P 〈 0.05). The mean levels of serum Dpt-specific IgG4 in all asthmatic groups were also significantly higher than in the non-allergic controls (P 〈 0.01). Moreover, the mean level of Dpt-specific IgG4 tended to increase during immunotherapy. A significant correlation between total serum IgG4 and Dpt-specirk IgG4 antibodies was noted (r= 0.6243; P 〈 0.001). Serial follow-up reveals that Dpt-specific IgG4 levels usually rose significantly with clinical improvement in asthmatic children during immunoiherapy. These results suggest that the anti-mite-specific IgG4 antibody may serve as an indicator for clinical outcome of mite allergy during immunotherapy.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2222.1991.tb01670.x
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  • 4
    Electronic Resource
    Electronic Resource
    Sequence analysis and expression of a cDNA clone encoding a 98-kDa allergen in Dermatophagoides farinae (1999)
    Oxford BSL : Blackwell Science Ltd
    Clinical & experimental allergy 29 (1999), S. 0 
    Details
    ISSN: 1365-2222
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The important dust mite allergens identified to date are of molecular weights ranging from 14 to 60 kDa. Our previous protein study indicated that the 98-kDa native paramyosin in Dermatophagoides farinae mite showed IgE reactivity with 82% of the mite-sensitive asthmatic patients suggesting that it is a novel major mite allergen. This study described the isolation and characterization of the cDNA clone encoding the 98-kDa mite allergen.〈section xml:id="abs1-2"〉〈title type="main"〉MethodsA Dermatophagoides farinae cDNA library was constructed in lambda ZAPII vector and the library was immunoscreened with a monoclonal antibody 642. The cDNA insert was sub-cloned into M13 sequencing vector for single-stranded sequencing. The whole cDNA insert was expressed in pGEX-2T Escherichia coli expression system as a fusion protein with GST. The allergenicity of the recombinant peptides was tested by skin tests and IgE immunoassay. The IgE and IgG immunoassays were performed with sera from 20 mite-allergic patients.〈section xml:id="abs1-3"〉〈title type="main"〉ResultsThe cDNA clone Df642 was 2134 bp long, coding for a polypeptide of 711 amino acid residues. Protein sequence analysis and alignment confirmed that the deduced polypeptide is a mite paramyosin which is truncated slightly at the N- and C-terminuses. In vivo skin tests and in vitro IgE-binding study showed that 62% (13/21) and 50% (10/20) of the mite-sensitive asthmatic patients reacted positively with the recombinant Dermatophagoides farinae paramyosin, respectively.〈section xml:id="abs1-4"〉〈title type="main"〉ConclusionThe study indicated that 98-kDa mite paramyosin is an important allergen.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2222.1999.00603.x
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  • 5
    Electronic Resource
    Electronic Resource
    The prevalence of allergic disease and IgE antibodies to house dust mite In schoolchildren in Taiwan (1990)
    Oxford, UK : Blackwell Publishing Ltd
    Clinical & experimental allergy 20 (1990), S. 0 
    Details
    ISSN: 1365-2222
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The prevalance of positive specific IgE antibodies to house dust mites (Dermatophagoides pteronyssinus: D. farinae) was determined by enzyme-linked immunosorbent assay (ELISA) in 5097 (61%) volunteers of 8345 schoolchildren aged between 7 and 14 yr from two government schools, All of them filled out a questionnaire concerning allergic symptoms. Among them, 412 (8·1%) children showed a positive reaction to at least one of the two mite allergens, the range varying between 5·6 and 11·2% according to the child's age. Boys had higher prevalence of positive mite specific IgE than girls (9·8% vs. 6·4%, P 〈 0·01), with the overall male to female ratio 1·5:1. The prevalence of bronchial asthma in boys and girls was 5·3% and 3·3% respectively. The positive mite specific IgE antibody in children with asthma and allergic rhinitis was 52% (103 of 198) and 28·7% (193 of 673) respectively. The mean levels of mite specific IgE were not significantly related to the age of onset and severity of asthmatic symptoms (P 〉 0·1), but were significantly different among subjects with current and past asthma (P 〈 0·001). It is suggested that the mire-specific IgE may play a role in the pathogenesis of bronchial asthma in children.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2222.1990.tb02772.x
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  • 6
    Electronic Resource
    Electronic Resource
    A unique human IgE-binding epitope on the Bermuda grass pollen recognized by mouse lambda-type 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: A group of six mouse monoclonal antibodies (MoAbs) with the unusual lambda-type light chain were generated by fusion of NS-1 cells with splenic cells derived from BALB/c mice immunized with crude extracts of Bermuda grass pollen (BGP). Four of them were IgG1, one was IgG2b, and one was IgG3. Binding inhibition assay showed that they recognized the same (or very similar) epitope. Using sera from BGP-allergic patients, it was found that the specific binding between the IgE antibodies and the MoAb 26–11-fixed antigen could be blocked by MoAb 26–11 itself and another MoAb 9–13 in a dose-dependent manner. It appears that the epitope recognized by the lambda-type MoAbs is a human IgE-binding antigenic determinant. Further physicochemical analyses showed that this epitope was stable under heat but sensitive to treatments of sodium periodate and proteinase K. Results from these studies indicate that this unique epitope which leads to the generation of lambda-type MoAbs is part of a glycoprotein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2222.1991.tb01692.x
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  • 7
    Electronic Resource
    Electronic Resource
    Characterization of the allergen Der f 7 from house dust mite extracts by species-specific and crossreactive monoclonal antibodies (1997)
    Oxford, UK : Blackwell Publishing Ltd
    Clinical & experimental allergy 27 (1997), S. 0 
    Details
    ISSN: 1365-2222
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Background The group 7 mite allergens react with IgE in 50% of sera from allergic patients.Objective To determine the molecular and antigenic characteristics and heterogeneity of Der f 7 in mite extracts.Methods Monoclonal antibodies (MoAbs) produced from mice immunized with recombinant Der f 7 were examined for crossreactivity to Der p 7 and then used for immunoblotting of 1 and 2-D gel electrophoresis. Deglycosylation was studied with N-glycosidase-F and N-terminal sequencing by Edman degradation. The epitopes of the monoclonal antibodies were compared by cross-inhibitory immunoassays.Results Immunoblotting of D. farinae extracts with all the anti Der f 7 MoAbs showed major reactivities at 31, 30 and 25 kDa. The strongest immunostaining was at 25 kDa which contrasted with Der p 7 where the 31 and 30 kDa bands were strongest. The relative strength of staining however varied between extracts. The 31 and 30 kDa components were glycosylation products of the 25 kDa form which had the N-terminal sequence predicted from cDNA analysis. Two MoAbs stained an 18 kDa band consistent with a degradation product. The 2-D gels showed that different components with pls from 5.6–6.4. Both species-specific and Der p 7 crossreactive MoAbs were produced and a two-site ELISA assay for detecting group 7 allergen was developed with MoAbs recognizing different epitopes.Conclusions Der f 7 has been defined by its natural N-terminal sequence and MoAbs. It apparently exists as different glycosylation and degradation products in mite extracts, the relative abundance of which differs with different preparations. A two-site ELISA to measure the allergen was developed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2222.1997.650890.x
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  • 8
    Electronic Resource
    Electronic Resource
    Protein sequence analysis of a novel 103-kDa Dermatophagoides pteronyssinus mite allergen and prevalence of serum immunoglobulin E reactivity to rDer p 11 in allergic adult patients (2004)
    Oxford, UK : Blackwell Science Ltd
    Clinical & experimental allergy 34 (2004), S. 0 
    Details
    ISSN: 1365-2222
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Background House dust mites are regarded as important indoor allergens. While the most studies mite allergens are low molecular weight (mw), a high mw Dermatophagoides farinae mite paramyosin (Der f 11) has recently been cloned. We have also cloned a novel high mw Dermatophagoides pteronyssinus (Dp) mite allergen, Der p 11.Objective The aim of this study was to isolate and express a cDNA gene coding for a Der p 11 allergen, to compare the sequence of Der p 11 with other antigens and to evaluate the presence of IgE reactivity to the recombinant protein (rDer p 11) in the sera of allergic adult patients.Methods The full-length Der p 11 gene was isolated by cDNA library screening, 5′-3′ rapid amplification of cDNA ends and PCR. The cDNA gene was expressed as a glutathione-S-transferase fusion protein in Escherichia coli. The allergenicity of rDer p 11 was tested by human IgE immunodot or immunoblot assay in a large panel of 100 allergic patients with bronchial asthma, allergic rhinitis or eczema.Results Der p 11 is a 2965 bp cDNA gene with a 2625 bp open reading frame coding for a 875 amino acid protein. The deduced amino acid sequence of the Der p 11 showed significant homology with various invertebrate paramyosins. The prevalence of serum IgE reactivity to rDer p 11 on immunodot assay ranged from 41.7% to 66.7% in different allergic patient groups, whereas it was rare in non-atopic patients with urticaria (18.8%) and in normal individuals (8%). A high frequency (five out of eight) of MAST(Dp)− allergic serum samples had specific IgE-binding activity to rDer p 11 or its fragments on immunoblot assay, even though their IgE-binding activity to Dp extract was either weak or negative.Conclusion The 103-kDa Der p 11 appears to be major Dp mite allergen with a high frequency of IgE reactivity in sera of patients allergic to mites.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2222.2004.01878.x
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  • 9
    Electronic Resource
    Electronic Resource
    Effect of ingestion of cow's milk hydrolysed formulas on whey protein-specific Th2 immune responses in naïve and sensitized mice (2004)
    Oxford, UK : Blackwell Science Ltd
    Clinical & experimental allergy 34 (2004), S. 0 
    Details
    ISSN: 1365-2222
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Background For genetically predisposed atopic infants, cow's milk protein hydrolysed formulas have been widely used.Objective Whether hydrolysed formulas can induce oral tolerance to whey proteins will be extensively studied in naïve and sensitized mice.Methods Antigenicity of hydrolysed formulas was first studied using immunoblotting. Naïve mice fed hydrolysed formulas for 1–4 weeks were sensitized with whey allergens. In contrast, mice sensitized with whey allergens were fed hydrolysed formulas continually for 12 weeks.Results Whey allergens were found in Nan and Neoangelac FL. Large whey peptides with antigenicity were found in Nan-HA. Profound suppression of IgE, IgG1 and IgG responses to whey allergens were induced in those fed Nan for 1 week, or Nan-HA for 4 weeks. IgE responses to whey allergens were suppressed in those fed Neoangelac FL for 4 weeks, or Nan-HA for 1–2 weeks. In contrast, those fed extensively hydrolysed formulas for 1–4 weeks failed to show decreased responses. On the other hand, IgE responses to β-lactoglobulin, but not to bovine serum albumin or α-lactalbumin, were decreased in sensitized mice fed Nan for 12 weeks. There was no suppression in sensitized mice fed hydrolysed formulas.Conclusion Suppression of IgE responses to whey proteins was readily induced in naïve mice fed Nan or Nan-HA for 1 week. In contrast, it was hardly induced in sensitized mice even after prolonged feeding of Nan for 12 weeks, let alone hydrolysed formulas.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2222.2004.1925.x
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  • 10
    Electronic Resource
    Electronic Resource
    Analysis of allergenic components of Bermuda grass pollen by monoclonal antibodies (1991)
    Oxford, UK : Blackwell Publishing Ltd
    Allergy 46 (1991), S. 0 
    Details
    ISSN: 1398-9995
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: A panel of 16 monoclonal antibodies (MoAbs) directed against Bermuda grass (Cynodon dactylon) pollen (BGP) were generated for identification and purification of the major allergenic components of the eliciting antigen (Ag). Radioimmunoprecipitation (RIP) analysis revealed that there were at least eight antigenic components with molecular weights (MW) ranging from 12 kilodalton (12 kDa) to 200 kDa. Each of these components has distinct biochemical characteristics based on sodium dodecyl sulfate – polyacrylamide gel electrophoresis (SDS-PAGE) and isoelectric focusing(IEF). Among them, Cyn d Bd67K and Cyn d Bd58K were basic proteins, Cyn d Bd35K consisted of at least four isomeric components with isoelectric points ranging from 6.2 to 7.2. The other antigens Cyn d Bd68K, 48K, 38K, Cyn d Bd200K, Cyn d Bd46K, Cyn d Bd25K and Cyn d Bd12K) were all acidic proteins. The IgE binding capacity of all these antigens was determined with sera from 11 BGP-allergics by using a modified radioallergosorbent test. All but one of the antigens (Cyn d Bd200K) were found to react with human IgE from sera of BGP-allergic patients. Among those human IgE-binding molecules, Cyn d Bd35K. reacted with allergic sera most frequently (10 of 11), followed by Cyn d Bd58K (8 of 11) and Cyn d Bd46K (7 of 11) respectively. Our results suggest that Cyn d Bd35K, Cyn d Bd58K, and Cyn d Bd46K are major allergens of BGP, and the MoAbs we obtained should be valuable tools for further purificaiton of these allergens.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1398-9995.1991.tb00615.x
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