Immunochemical Crossreactivity between Globulins from Buckwheat and Indigo Seeds

Takumi, Kenji; Koga, Tetsuro; Kanoh, Makoto; Udaka, Junko; Tsuji, Hideaki; Manabe, Shoichi

doi:10.1271/bbb.59.1971

Cited by 5 publications

(3 citation statements)

References 3 publications

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“…Inhalation or ingestion of a very small amount of buckwheat allergens can initiate severe symptoms in patients with hypersensitivity to buckwheat. 1 The immunologic properties of buckwheat allergens have been studied by several investigators, [2][3][4][5][6][7][8][9][10][11] but their molecular natures are still unclear. Yanagihara has described buckwheat allergen proteins with molecular masses of approximately 100, 50 and 17 kDa.…”

Section: Introductionmentioning

confidence: 99%

Molecular characterization of buckwheat major immunoglobulin E-reactive proteins in allergic patients

Nagata

Fujino

Hashiguchi

et al. 2000

Allergology International

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Buckwheat extract was analyzed by immunoblotting experiments using sera from nine allergic and three non‐allergic individuals. Major IgE‐reactive bands were 73, 70, 62, 58 and 54 kDa under non‐reducing conditions and were detected in allergic subjects, but not in non‐allergic ones. Under reducing conditions, the 73, 70, 62 and 58 kDa bands split to 56 and 24, 52 and 24, 45 and 24, and 43 and 24 kDa, respectively. The 24 kDa molecule was the most prominent band recognized with IgE as well as IgG or IgA. The FA02 cDNA clone, encoding the α and β subunits of the legumin‐like storage protein, was isolated from a cDNA library made of immature buckwheat seeds. The deduced amino acid sequence of the cDNA clone is substantially identical to the N‐terminal amino acid sequence of the 24 kDa molecule, which may be identical to that of BW24KD reported by Urisu et al. Consistent with these results, the translation product of the cDNA encoding the putative β subunit was strongly recognized with serum IgE, IgG and IgA from buckwheat‐allergic patients. These results suggested that the 24 kDa molecule may be the β subunit of the legumin‐like storage molecule of buckwheat.

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Section: Introductionmentioning

confidence: 99%

Molecular characterization of buckwheat major immunoglobulin E-reactive proteins in allergic patients

Nagata

Fujino

Hashiguchi

et al. 2000

Allergology International

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“…Buckwheat (BW) allergens initiate severe symptoms including wheezing, urticaria, vomiting, and anaphylactic shock in patients with hypersensitivity to BW (1, 2). Several BW molecules recognized by serum immunoglobulin E (IgE) derived from allergic patients have been reported (3–15). Yanagihara reported proteins with molecular mass of 100, 50, and 17 kDa as BW allergens (11).…”

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Molecular characterization of a 10‐kDa buckwheat molecule reactive to allergic patients’ IgE

Matsumoto

Fujino

Nagata

et al. 2004

Allergy

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“…These data strongly-suggest that the starch-storing cereals or tu bers share the buffer A-soluble glutelin components. As for the immunochemical relationship between MG60 and GBSS, this was examined by immunoblot analysis (15) using rabbit anti-MG60 antiserum that was pre pared by a procedure described previously (16). At first, the antigenic specificity of the antiserum to anti-MG60 was determined against several millet proteins as shown in Fig.…”

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Structural and Immunochemical Homologies between Foxtail Millet Glutelin 60 kDa and Starch Granule-bound Starch Synthase Proteins from Rice, Barley, Corn and Wheat Grains.

Takumi¹,

Udaka²,

Kimoto³

et al. 2000

Journal of Nutritional Science and Vitaminology, J Nutr Sci Vit

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SummaryFoxtail millet glutelin 60kDa (MG6O) was purified by preparative SDS-PAGE, and the N-terminal amino acid sequence was determined within 20 residues. The result demonstrated that the primary structure at N-terminal of MG60 was almost identical to those of the granule-bound starch synthase (GBSS) proteins from rice, barley, corn, wheat and potato. The existence of common epitopes among MG60 and GBSS proteins from these starch-storing cereals were corroborated by immunoblot analysis using antisera raised against MG60. These facts strongly suggest a close relationship between MG60-like glutelins and GBSS proteins. Key Words foxtail millet, glutelin 60kDa, N-terminal amino acid sequence, starch gran ule-bound starch synthase, antigenic homology.Our previous paper (1) indicated that the prolamins from foxtail (Italian), proso (Common) and sawa (Japanese) millet cultivars contained common epitopes among them. Since then, however, little information on the physico-or immuno-chemical properties of the mil let storage proteins has been published so far as we know. Miflin and Shewry (2) have proposed that glutelin proteins serve a metabolic and/or structural role rather than a storage function in some cereals. Recently, we purified a polypeptide a component with a molecular mass (MM) of 60 kDa (referred to as MG60) from the urea-soluble glutelin of a foxtail millet cultivar. Then, the N-terminal amino acid sequence of MG60 was determined by the method of Matsudaira (3) in order to obtain the first clue about the function of the newly obtained glutelin component.

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Immunochemical Crossreactivity between Globulins from Buckwheat and Indigo Seeds

Cited by 5 publications

References 3 publications

Molecular characterization of buckwheat major immunoglobulin E-reactive proteins in allergic patients

Molecular characterization of buckwheat major immunoglobulin E-reactive proteins in allergic patients

Molecular characterization of a 10‐kDa buckwheat molecule reactive to allergic patients’ IgE

Structural and Immunochemical Homologies between Foxtail Millet Glutelin 60 kDa and Starch Granule-bound Starch Synthase Proteins from Rice, Barley, Corn and Wheat Grains.

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