Measurement of the potency of allergy extracts by their inhibitory capacities in the radioallergosorbent test

Gleich, Gerald J.; Larson, James B.; Jones, Richard T.; Baer, Hans H.

doi:10.1016/0091-6749(74)90004-9

Cited by 199 publications

(55 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Since these subjects have positive skin and RAST reactions to crab, crawfish and lobster in addition to shrimp even though they report no exposure to nonshrimp species [36, 37], cross–sensitivity among crustaceans may exist. RAST inhibition and cross–immunoelectrophoresis studies [38, 39, 40]were first used to demonstrate cross–reactive allergens among crustacean species that was not due to multiple sensitization. In RAST inhibition studies, shrimp was the most potent inhibitor of the IgE directed to shrimp, followed in potency by crawfish, lobster and crab [39].…”

Section: Cross–reactivity Among Tropomyosins In Different Speciesmentioning

confidence: 99%

Tropomyosin: An Invertebrate Pan–Allergen

Reese

Ayuso

Lehrer³

1999

Int Arch Allergy Immunol

453

299

View full text Add to dashboard Cite

Among food allergens, crustaceans, such as shrimp, crab, crawfish and lobster, are a frequent cause of adverse food reactions in allergic individuals. The major allergen has been identified as the muscle protein tropomyosin. This molecule belongs to a family of highly conserved proteins with multiple isoforms found in both muscle and nonmuscle cells of all species of vertebrates and invertebrates. Its native structure consists of two parallel alpha–helical tropomyosin molecules that are wound around each other forming a coiled–coil dimer. Allergenic tropomyosins are found in invertebrates such as crustaceans (shrimp, lobster, crab, crawfish), arachnids (house dust mites), insects (cockroaches), and mollusks (e.g. squid), whereas vertebrate tropomyosins are nonallergenic. Studies of cross–reactivities among crustaceans and the high degree of sequence identity among them suggest that tropomyosin is probably the common major allergen in crustaceans. Furthermore, immunological relationships between crustaceans, cockroaches and housedust mites have been established and may suggest tropomyosin as an important cross–sensitizing pan allergen.

show abstract

Section: Cross–reactivity Among Tropomyosins In Different Speciesmentioning

confidence: 99%

Tropomyosin: An Invertebrate Pan–Allergen

Reese

Ayuso

Lehrer³

1999

Int Arch Allergy Immunol

453

299

View full text Add to dashboard Cite

show abstract

“…RAST inhibition was carried out essentially as described by Gleich et al [30]: allergosorbent discs were incubated with 50 pi of the sample to be tested together with 12 pi of the serum pool over night at room temperature: bound IgE was evaluated as previously described. The inhibition percentage was calculated using the for mula:…”

Section: Radioallergosorbent Testmentioning

confidence: 99%

Purification and Characterization of Par· I, Major Allergen of Parietaria officinalis Pollen

Oreste

Coscia²,

d’Abusco³

et al. 1991

Int Arch Allergy Immunol

View full text Add to dashboard Cite

Par·I, a major allergen of Parietaria officinalis, was purified from the pollen extract. The purified allergen was obtained by ultrafiltration, Sephadex gel filtration and DE-52 ion exchange chromatography: the purified preparation yields a single band in polyacrylamide gel isoelectric focusing (PAG-IEF), sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) and immunoblotting, a single immunoprecipitation arc in crossed immunoelectrophoresis (CIE) and crossed radioimmunoelectrophoresis (CRIE) and a single peak in size exclusion high-performance liquid chromatography (HPLC). Par·I is a glycoprotein with a protein to carbohydrate ratio of 100:21. The molecular weight, determined by SDS-PAGE, Sephadex G-50 gel filtration and size exclusion HPLC, varied between 13.5 and 14.5 kDa according to the method employed. The isoelectric point was 4.6. The amino acid composition and the sequence of the first twelve N-terminal residues were determined. The allergenicity was assayed in vivo and in vitro. 29/29 Parietaria-allergic patients were skin positive to Par·I and possessed high level of specific serum IgE antibody as it determined by radioallergosorbent test (RAST). Par·I contained dominant epitopes for human IgE as inhibited to 85% the pollen extract RAST performed with a pool of sera of allergic patients. The RAST inhibitory activity was not abolished by deglycosylation.

show abstract

“…The aller genicity of each fraction was tested by RAST di rect technique [15]; the potency of the allergenici ty was determined by RAST inhibition [7] and his tamine release-inhibition [13] from human allergic leukocytes and mast cells from rats sensitized with WAE included in Bordetella pertussis vaccine. The ID50 was the concentration which caused 50% inhibition of RAST or histamine release.…”

Section: Methodsmentioning

confidence: 99%