Manufacturers' criteria for in-house references.
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Allergens↗
Biomedical subjects
R Einarsson
Publications and source records attributed to R Einarsson.
IgG and IgE antibody patterns after immunotherapy with monomethoxy polyethyleneglycol modified honey bee venom.
Antibody responses to honey bee venom (HBV) were studied in 13 patients during a 4-month course of immunotherapy with monomethoxy polyethyleneglycol (mPEG) modified venom. There was a rise of HBV-specific IgG antibodies as measured by IgG-RAST in all patients and a slight decrease of IgE antibody in most of them. The IgG-antibody responses during mPEG-HBV treatment as examined by crossed radioimmunoelectrophoresis were directed to phospholipase A, hyaluronidase, acid phosphatase and to another allergen, antigen 1. Thus, despite a high degree of mPEG-modification of HBV, the immunogenicity of the most important HBV allergens was retained.
Adult↗
A double-blind, multicenter immunotherapy trial in children, using a purified and standardized Cladosporium herbarum preparation. II. In vitro results.
This double-blind immunotherapy trial in children, using a purified and standardized Cladosporium herbarum allergen preparation, has shown that children with mould asthma and/or rhinoconjunctivitis, responded to immunotherapy with a decrease in specific IgE and a significant increase in specific IgG. There was a marked increase in the ratio specific IgG/specific IgE as a result of active treatment. IgE-CRIE radiostaining patterns showed no pronounced changes after 10 months' active treatment and no "new sensitivities" could be detected in the studied patients. IgG-CRIE radiostaining, primarily directed towards the important allergens, was significantly increased in the active group and particularly towards Ag-12 (partially identical to a previously described major allergen in Cladosporium herbarum, Ag-54). Children treated with histamine placebo showed no change in antibody patterns during 10 months of treatment.
Adolescent↗
Detection of allergens in mould and mite preparations by a nitrocellulose electroblotting technique.
The allergen composition of moulds (Alternaria alternata and Aspergillus fumigatus) and mites (Dermatophagoides pteronyssinus and Dermatophagoides farinae) was studied by electroblotting. The allergens were separated by SDS-gPAGE and transferred to a nitrocellulose membrane by electroblotting. Specific IgE antibodies directed against mould and mite allergens were utilized as probes to detect the allergens. The bands were localized on the nitrocellulose membrane by means of enzyme- or isotope-labelled antibody. Circulating specific IgE antibodies in mould and mite sensitive patient sera were also analyzed and characterized with respect to their IgE specificity. Under appropriate experimental conditions this electroblotting technique could also be used for quantitation of individual allergens by scanning the isotope- or enzyme-stained nitrocellulose strips.
Allergens↗
Crossed immunoelectrophoresis and crossed radioimmunoelectrophoresis analysis of "yellow jacket-common wasp" (Vespula spp.).
Crossed immunoelectrophoresis (CIE) pattern of Yellow jacket vespid venom showing 25 immunoprecipitates was used in crossed radioimmunoelectrophoresis (CRIE) analysis with sera from 35 subjects allergic to vespid venom. Phospholipase A and B, hyaluronidase, acid and alkaline phosphatases and a lytic active component were demonstrated in immunoprecipitates using zymography and direct haemolysis of sheep erythrocytes. CRIE analysis proved the allergenicity of these proteins. In addition, another antigen (Ag 17) with no detectable enzymatic or lytic activity was identified as an important allergen. This allergen is most likely identical to the previously described Antigen 5 in vespid venoms. By using CIE/CRIE the presence and complexity of multiple forms of the allergenic protein components were well demonstrated.
Allergens↗
Biochemical and immunochemical methods for purification, characterization and standardization of allergen extracts.
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Allergens↗
Characterization of allergens and patient sera by a nitrocellulose immunoprint technique.
A rapid and convenient protein-gel blot technique for qualitative detection of antigens/allergens in pollen allergen extracts and IgE/IgG antibodies in patient sera has been developed. The antigens were separated by isoelectric focusing in agarose gel and transferred to nitrocellulose by capillary migration. After incubation of the nitrocellulose strips with serum from allergic patients, the binding of the patient's specific IgE or IgG antibodies was analyzed by using isotope-labelled or enzyme-labelled anti-IgE or anti-IgG. The time needed for detection with isotope-labelled antibody was approximately 20 h and with enzyme-labelled antibody 2 h. The immunoprint technique is easy to use, which renders it suitable for routine use in allergy research and quality control.
Allergens↗
Mold allergy--spores and mycelium as allergen sources.
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Allergens↗
Use of capillary isotachophoresis to measure the degree of chemical substitution of dog serum albumin.
Analytical capillary isotachophoresis may provide a means for the rapid determination of the degree of substitution of proteins. Dog albumin conjugates with trinitrophenyl (TNP), fluorescein isothiocyanate (FITC) or monomethoxy polyethylene glycol (mPEG) have been studied as models for protein modification. An increase in the degree of covalent substitution of dog albumin with TNP, FITC or mPEG could be monitored rapidly using the UV signal or the conductivity signal as a measure of the increased protein zone width. These findings are encouraging with regard to the possible use of capillary isotachophoresis for screening the extent of protein modification.
Animals↗
Ion-exchange chromatographic characterization of stinging insect vespid venoms.
Paper wasp, hornets and yellow jacket vespid venoms were analysed by electrofocusing-electrophoresis titration curves and cation exchange chromatography on Mono STM. Important protein components were identified by zymography. The elution profiles from the cation exchange column for the different vespid venoms differed significantly, demonstrating the use of this technique for identification purposes. The various fractions from the ion-exchange elution profiles were collected and analysed with respect to enzymatic activity. The high capacity of the system makes it also suitable for preparative scale separation.
Acid Phosphatase↗
Bee keepers' IgG and IgE antibody responses to bee venom studied by means of crossed radioimmunoelectrophoresis.
The immune response to honey bee venom in thirty-seven bee keepers' sera was studied by several methods. Specific IgE antibody levels studied by RAST were generally low, whereas specific IgG antibody levels studied by a Sepharose protein A technique were high. Crossed radioimmunoelectrophoresis was applied for a detailed analysis of the antibody specificities towards the different components of venom in seventeen of the bee keepers' sera. Significant amounts of IgG antibodies were found towards most bee-venom components. The highest IgG response was directed towards phospholipase A. Hyaluronidase, acid phosphatase and two uncharacterized antigens also showed distinct IgG binding. The IgG binding to melittin was low. The IgE binding to the bee venom components was low and primarily directed to the phospholipase. IgE binding to hyaluronidase and acid phosphatase occurred, but was also in very small amounts. One bee-keeper serum caused heavy radiostaining to melittin but the others did not show IgE binding to this component. Thus a low IgE but a high IgG response was demonstrated in bee keepers. The major immunogen was phospholipase A, which is known to be the major allergen in bee venom. Generally, the strongest IgG responses were found to the components capable of inducing the strongest IgE responses.
Adult↗
Antigenic/allergenic composition of Poodle/Alsatian dandruff extract.
Poodle and Alsatian dog dandruff extracts were characterized by crossed immunoelectrophoresis (CIE) and crossed radioimmunoelectrophoresis (CRIE) using sera from 24 individuals clinically sensitive to dogs. By using a system with intermediate gel in immunoelectrophoresis, the content of dander-specific and serum-specific allergens was established. 29 antigens (18 dander-specific and 11 serum-specific) were identified in the mixed breed Poodle/Alsation dandruff extract. Of these, 24 antigens were radiostained in CRIE. 16 allergens were dander specific and the remaining eight were serum specific. Positive dog dander RAST (e5 and Poodle/Alsatian dandruff extract) results were observed in the tested dog hypersensitive subjects. Our results suggest that the mixture of Poodle/Alsatian dandruff extract may be a suitable preparation for the diagnosis and treatment of dog allergy.
Allergens↗
Antigenic variability of different strains of Aspergillus fumigatus.
10 strains (isolates) of Aspergillus fumigatus, grown and harvested under identical conditions, were compared with respect to biochemical and immunological properties. The total protein and carbohydrate content isoelectric focusing pattern were determined for each of the individual strains. Their antigenic and allergenic activity was examined by a combination of crossed immunoelectrophoresis (CIE)/crossed radioimmunoelectrophoresis (CRIE) and RAST inhibition. Biochemical and immunochemical data indicated that considerable variation exists between the various isolates of A. fumigatus. 44 antigens were demonstrated in CIE of A. fumigatus, and 18 different allergens were identified in CRIE (2 major, 10 intermediate and 6 minor allergens).
Animals↗
Crossed radioimmunoelectrophoretic analysis of cultivated rye (Secale cereale) pollen allergens.
Cultivated rye pollen extracts were characterized by means of crossed immunoelectrophoresis (CIE) and crossed radioimmunoelectrophoresis (CRIE). 32 antigens were identified in CIE and among these 16 were radiostained in CRIE analysis of a rye pollen sensitive patient panel. Crossed line immunoelectrophoresis revealed that some of the rye pollen antigens were immunological partially identical with antigens of wheat flour and rye flour.
Animals↗
Determination of specific IgG antibody by crossed radioimmunoelectrophoresis.
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Animals↗
A rapid procedure for crossed radio immunoelectrophoresis.
A procedure for performing crossed radio immunoelectrophoresis (CRIE) with significantly reduced exposure times has been developed. The rapid method has been effected by using a highly sensitive X-ray film (Du Pont Cronex-4) and X-ray intensifying screen (Du Pont Lighting Plus) and by exposing at low temperatures (-70 degrees C) in a Kodak X-Omatic cassette. Exposure at -70 degrees C appears to be critical to obtain optimal radiostaining. Furthermore, the isotope concentration has been increased from 250,000 to 500,000 cpm without any loss of specificity or reproducibility. The rapid CRIE procedure makes it possible to obtain a CRIE screening within 1 day and, furthermore, a complete CRIE classification (CRIE classes A-G) within 5 days.
Antibodies, Anti-Idiotypic↗
Crossed radioimmunoelectrophoretic studies of bee venom allergens.
Crossed immunoelectrophoresis (CIE) glass slides of honey bee venom showing 18 immunoprecipitates were used in crossed radioimmunoelectrophoresis (CRIE) experiments with sera from 25 patients allergic to honey bee venoms. Phospholipase A, acid phosphatase, hyaluronidase and melittin were demonstrated in the immunoprecipitates using zymographic techniques and direct hemolysis of sheep erythrocytes. The CRIE experiments verified the allergenicity of these proteins. In addition, another antigen (Ag-1) with allergenic activity was identified. This allergen is probably identical to the previously described allergen C in honey bee venom. The presence and complexity of multiple forms of the known allergenic proteins in honey bee venom, was well illustrated in the CIE/CRIE system employed.
Allergens↗
Crossed Immunoelectrophoresis analysis of bee venom. Enzymatic identification of antigens.
Bee venom obtained by electrical stimulation has been analysed by crossed immunoelectrophoresis against high-titer rabbit antibodies. The antigenic analysis of bee venom revealed that the extract contained 17 antigens, which were detected in the crossed immunoelectrophoresis pattern after staining with Coomassie Brilliant Blue. The crossed immunoelectrophoresis pattern indicated heterogeneity in several of the antigens, as most of the precipitates (exhibiting enzyme and hemolytic activities) represented multiple forms of phospholipase A, hyaluronidase, acid phosphatase and melittin.
Acid Phosphatase↗