Gastrointestinal digestion and absorption of Pen j 1, a major allergen from Kuruma prawn, Penaeus japonicus.

Tropomyosin had been identified as a major allergen in shrimp. The digestion and absorption of tropomyosin (Pen j 1) from kuruma prawn were investigated by ex vivo, in vitro, and in vivo techniques in order to elucidate the relationship between the allergenicity of the allergen and its gastrointestinal behavior. Pen j 1 transported the Caco-2 monolayer in a dose-dependent manner, and also enhanced the permeability of lucifer yellow, a marker of paracellular transportation, at high concentrations of the allergen.

Investigation of multiple forms of Tri a Bd 27K, a major wheat allergen, by immunoblotting analysis.

Tri a Bd 27K, a major wheat allergen, is a glycoprotein. Tri a Bd 27K was found to occur in multiple forms by two-dimensional polyacrylamide gel electrophoresis and immunoblotting with a monoclonal antibody against the allergen. Furthermore, it was found that only Tri a Bd 27K components, which have N-linked glycan moieties with fucose residues, bound to IgE antibodies in the sera of wheat-sensitive patients.

Preparation and epitope mapping of a monoclonal antibody against Tri a Bd 27K, a major wheat allergen.

We produced a monoclonal antibody (mAb) as a probe for detection of Tri a Bd 27K, a major wheat allergen. The mAb recognized the allergen purified from wheat flour, and the epitope on the allergen to the mAb was determined to be amino acid sequence (154)VPWVVVDGKPL(164) of Tri a Bd 27K. Of the amino acid residues on the epitope, the amino acid residues responsible for the binding to the mAb were found to be W156, D160, G161, and P163.

Development of a method for the determination of gamma-aminobutyric acid in foodstuffs.

A method for the determination of gamma-aminobutyric acid (GABA) in foodstuffs has been developed by combination of its dinitrophenylation and high-performance liquid chromatography (HPLC) using norleucine as an internal standard. GABA was converted to its stable derivative with 1-fluoro-2,4-dinitrobenzene and the derivative was extracted with ether. After evaporation of the extract, the residue was dissolved in 0.

Molecular cloning and allergenicity of Pen j 1, a major allergen of kuruma prawn, Penaeus japonicus.

Tropomyosins have been identified as a common allergen in crustaceans, but their allergenicity is not well understood. In the present study, we isolated an allergen, Pen j 1, a tropomyosin from kuruma prawn Penaeus japonicus, and determined its N-terminal amino acid sequence. The cDNA encoding the allergen was cloned by 5'- and 3'-rapid amplification of cDNA ends (RACE), and was found to code for a protein which consists of 284 amino acid residues.