juglans hindsii/albumine

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Identification and characterisation of the IgE-binding proteins 2S albumin and conglutin gamma in almond (Prunus dulcis) seeds.

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BACKGROUND Almond proteins can cause severe anaphylactic reactions in susceptible individuals. The aim of this study was the identification of IgE-binding proteins in almonds and the characterisation of these proteins by N-terminal sequencing. METHODS Five sera were selected from individuals with a

Lipid transfer proteins and 2S albumins as allergens.

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Plant lipid transfer proteins, a widespread family of proteins, have been recently identified as important food allergens. Their common structural features, such as eight conserved cysteines forming disulfide bridges, basic isoelectric point and high similarity in amino acid sequence, are the basis

Expression of Jug r 1, the 2S albumin allergen from walnut (Juglans regia), as a correctly folded and functional recombinant protein.

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Jug r 1, the 2S albumin allergen from walnut, was isolated from ripe nuts as a native allergen and expressed in Escherichia coli using the Gateway technology as a recombinant allergen. The recombinant Jug r 1 (15 kDa) differs from the native allergen by the absence of cleavage of the polypeptide

Eco-friendly walnut shell powder based facile fabrication of biogenic Ag-nanodisks, and their interaction with bovine serum albumin.

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Walnut shell biomass was used for the extraction of juglone by water as a solvent at room temperature. Upon addition of AgNO₃ to a dye solution, prefect transparent pale brown color develops within the reaction time. UV-visible spectroscopy revealed the appearance of surface plasmon

Cloning and sequencing of a gene encoding a 2S albumin seed storage protein precursor from English walnut (Juglans regia), a major food allergen.

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BACKGROUND Walnuts rank third in per capita consumption of tree nuts in the United States and can be associated with systemic IgE-mediated reactions in some individuals. OBJECTIVE The objectives of the study were to clone a gene encoding one of the major food allergens in the walnut kernel and to

Ana o 3, an important cashew nut (Anacardium occidentale L.) allergen of the 2S albumin family.

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BACKGROUND Cashew nut allergy is the second most commonly reported tree nut allergy in the United States. We have previously cloned and characterized major cashew allergens belonging to the vicilin and legumin families of seed storage proteins. OBJECTIVE Here we set out to describe a third major

Cloning and characterization of 2S albumin, Car i 1, a major allergen in pecan.

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Although pecans are associated with IgE-mediated food allergies, the allergens responsible remain to be identified and characterized. The 2S albumin gene was amplified from the pecan cDNA library. Dot-blots were used to screen the recombinant protein with pecan allergic patients' serum. The affinity

Determination of walnut protein in processed foods by enzyme-linked immunosorbent assay: interlaboratory study.

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Because food allergens from tree nuts, including walnuts, are a frequent cause of adverse food reactions for allergic patients, the labeling of foods containing ingredients derived from tree nuts is required in numerous countries. According to Japanese regulations, the labeling of food products

Gamma scintigraphic analysis of the distribution of perfusion of blood in the equine foot during black walnut (Juglans nigra)-induced laminitis.

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Twelve horses, with acute laminitis (primarily in the forefeet) at 12 hours after intragastric dosing with an aqueous extract of black walnut (Juglans nigra) heart-wood, were studied. The distribution of perfusion of blood to the foot and to outlined regions within the foot was quantified, using

Extensive in vitro cross-reactivity to seed storage proteins is present among walnut (Juglans) cultivars and species.

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BACKGROUND Tree nuts, including English walnuts (Juglans regia), are sources of food allergens often associated with life-threatening allergic reactions. It is unknown if seed storage proteins from other Juglans species have IgE epitopes similar to those of the important English walnut allergens,

Hepatoprotective effects of Juglans regia extract against CCl4-induced oxidative damage in rats.

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BACKGROUND Different parts of the walnut [Juglans regia L. (Juglandaceae)] have been used in folk medicine for protection against liver injury, although its actual efficacy remains uncertain. OBJECTIVE The present study investigated the protective effect of walnut leaf extract against carbon

Protein Hydrolyzates from Changbai Mountain Walnut (Juglans mandshurica Maxim.) Boost Mouse Immune System and Exhibit Immunoregulatory Activities.

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The Changbai Mountain walnut (Juglans mandshurica Maxim.) is a rich source of essential amino acids. Walnut dregs are byproducts of edible oil production and primarily used as fodder and fertilizers. We systematically examined the effect of three types of walnut protein hydrolyzates-albumin,

Characterization of low molecular weight allergens from English walnut (Juglans regia).

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Although English walnut is a commonly allergenic tree nut, walnut allergens have been poorly characterized to date. The objective of this work was to characterize the natural, low molecular weight (LMW) allergens from walnut. A protocol was developed to purify LMW allergens (specifically 2S

Toxicological Effects of Aqueous Extract From African Walnut ( Tetracarpidium conophorum) Leaves in Rats.

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Tetracarpidium conophorum leaves are used in traditional medicine for the treatment of male infertility, without considering its toxicity and side effects. In this study, we investigated the effects of T conophorum leaves on some biochemical parameters such as alanine aminotransferase, aspartate

Characterization of the soluble allergenic proteins of cashew nut (Anacardium occidentale L.).

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The allergens associated with cashew food allergy have not been well-characterized. We sought to identify the major allergens in cashew nut by performing IgE immunoblots to dissociated and reduced or nonreduced cashew protein extracts, followed by sequencing of the peptides of interest. Sera from 15

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