arachis hypogaea/albumin

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Structure and stability of 2S albumin-type peanut allergens: implications for the severity of peanut allergic reactions.

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Resistance to proteolytic enzymes and heat is thought to be a prerequisite property of food allergens. Allergens from peanut (Arachis hypogaea) are the most frequent cause of fatal food allergic reactions. The allergenic 2S albumin Ara h 2 and the homologous minor allergen Ara h 6 were studied at

Transient expression of GUS and the 2S albumin gene from Brazil nut in peanut (Arachis hypogaea L.) seed explants using particle bombardment.

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The effect of parameters involved in the transformation efficiency of peanut (Arachis hypogaea L.) seed tissues by direct gene transfer using a helium inflow particle bombardment device was evaluated. Transient gene expression was affected by both particle and DNA amounts, and was positively

Some 2S albumin from peanut seeds exhibits inhibitory activity against Aspergillus flavus.

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A crude 2S albumin fraction was separated from peanut (Arachis hypogaea L.) cotyledons. Untreated 2S albumin had little inhibitory activity against trypsin, spore germination, or hyphal growth of Aspergillus flavus. However, following treatment of 2S albumin with SDS, increased inhibitory activity

The 2S albumin allergens of Arachis hypogaea, Ara h 2 and Ara h 6, are the major elicitors of anaphylaxis and can effectively desensitize peanut-allergic mice.

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BACKGROUND Ara h 2 and Ara h 6, co-purified together in a 13-25 kD fraction (Ara h 2/6; 20 kD fraction) on gel filtration chromatography, account for the majority of effector activity in a crude peanut extract (CPE) when assayed with RBL SX-38 cells sensitized with IgE from human peanut allergic

Localization of lectin-binding sites and sugar-binding proteins in tachyzoites of Toxoplasma gondii.

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Lectins and neoglycoproteins labeled with colloidal gold particles were used for the ultrastructural localization of carbohydrate residues and sugar-binding sites, respectively, in thin sections of tachyzoites of Toxoplasma gondii embedded in the Lowicryl K4M resin. Incubation of the sections in the

Detection of the cancer-associated T antigen using an Arachis hypogaea agglutinin biosensor.

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An impedimetric biosensor was developed for the selective detection of the cancer-associated T antigen, using the lectin from Arachis hypogaea (peanut agglutinin, PNA) as the recognition element. The increase in the biosensor's impedance after sample incubation was indicative of lectin recognition

Site-specific monoclonal antibodies against peanut agglutinin (PNA) from Arachis hypogaea. Immunohistochemical study of tissue-cultured cells and of 27 cases of Hodgkin's disease.

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The purpose of this study was to increase the sensitivity of the staining reaction for the T antigen on the surface of neoplastic cells grown in vitro with the use of site-specific monoclonal antibodies (MAbs). The authors describe anti-peanut agglutinin (PNA) MAbs selected by screening the

Isolation and characterization of amaranthin, a lectin present in the seeds of Amaranthus caudatus, that recognizes the T- (or cryptic T)-antigen.

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A lectin (Amaranthin) present in the seeds of Amaranthus caudatus has been isolated by fractionation on DEAE-cellulose followed by affinity chromatography on Synsorb-T beads (Gal beta 1,3GalNAc alpha-O-R-Synsorb). The lectin appeared homogeneous by gel electrophoresis at pH 4.3 and gave a single

Glyco-macroligand microarray with controlled orientation and glycan density.

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We report a new type of glycan microarray, namely, oriented and density-controlled glyco-macroligand microarray based on end-point immobilization of glycopolymer that was accompanied with boronic acid (BA) ligands in different sizes as detachable "temporary molecular spacers". Briefly, an O-cyanate

Seed protein fraction electrophoresis in peanut (Arachis hypogaea L.) accessions and wild species.

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Total seed storage proteins were studied in 50 accessions of A. hypogaea (11 A. hypogaea ssp. hypogaea var hypogaea, 13 A. hypogaea ssp. hypogaea var hirsuta, 11 A. hypogaea ssp. fastigiata var fastigiata and 15 A. hypogaea ssp. fastigiata var. vulgaris accessions) in SDS PAGE. These accessions were

4-methyleneglutamine amidohydrolase from peanut leaves : preparation, catalytic properties, and immunological responses of a highly purified form of the enzyme.

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4-Methyleneglutamine amidohydrolase has been extracted and purified over 1000-fold from 14-day-old peanut (Arachis hypogaea) leaves by modification of methods described previously. The purified enzyme shows two bands of activity and three to four bands of protein after electrophoresis on

Identification and characterisation of seed storage protein transcripts from Lupinus angustifolius.

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BACKGROUND In legumes, seed storage proteins are important for the developing seedling and are an important source of protein for humans and animals. Lupinus angustifolius (L.), also known as narrow-leaf lupin (NLL) is a grain legume crop that is gaining recognition as a potential human health food

Benefits and limitations of molecular diagnostics in peanut allergy: Part 14 of the series Molecular Allergology.

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Allergic reactions to peanut (Arachis hypogaea, Ara h) are caused by immunoglobulin E (IgE)-mediated sensitizations to various proteins. The stability and relative proportion of these proteins in peanut determine the risk of hazardous reactions. Hazardous sensitization to seed storage proteins [S2

Early development of the representation of the body surface in SI cortex barrel field in neonatal rats as demonstrated with peanut agglutinin binding: evidence for differential development within the rattunculus.

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Physiological studies have demonstrated a highly organized somatotopic representation of the body surface in SI cortex of rat. This representation is correlated morphologically with the presence of barrel-shaped structures in layer IV. Conventional staining techniques reveal barrels in the latter

Isolation, characterization and implications of anti-TF (Thomsen-Friedenreich) agglutinins from different sources.

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Anti-TF agglutinins from peanut (Arachis hypogaea) and from vertebrate sera of different species have been successfully isolated by affinity chromatography on acid-activated Sepharose 4 B. The proteins were characterized by immunoelectrophoresis, polyacrylamide gel electrophoresis in the presence of

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