Sweet Almond Oil 100ml - Cold Pressed & Unrefined - 100% Natural - Prunus Amygdalus Dulcis Oil - Italy - Best Care Oil for Skin - Hair - Body - Personal Care - Glass Bottle

Product Information

Sathe et al. (2001) [ 730] used 13% acrylamide 1D gels for separation. Samples were reduced with beta-mercaptoethanol and heated. Process, chemical, enzymatic: Not known but the disulphide linked alpha-helical structures of this protein family is likely to be very stable.

Allergen purification: Defatted almond flour was extracted with 10 volumes of 0.02 M Tris-HCl (pH 8.1 buffer) with constant magnetic stirring, filtered through glass wool, and the filtrate was centrifuged. The supernatant was loaded onto a DEAE DE-53 column equilibrated in 0.02 M Tris-HCl buffer and then eluted with a 0-0.5 M NaCl gradient. Fractions containing the almond major protein, AMP, were pooled and concentrated. Aliquots were loaded on a Sephacryl S300 column in Tris buffer with 0.1 M NaCl. Fractions containing the AMP were pooled, dialyzed, and lyophilized (Acosta et al. 1999 [ 732]). Prunin, described as the major storage protein of almond (Garcia-Mas et al., 1995 [ 923]), is taken above as a synonym of amandin. A voluntary registry for peanut and tree nut allergy: characteristics of the first 5149 registrants. Poltronieri et al. (2002) [ 725] used 10-12% acrylamide (or 16% to resolve low molecular mass proteins) 1D gels for separation.

#Product Details#

Many studies report allergy to "tree nuts". Allergy to almond was the third most common of the tree nuts reported by Sicherer et al. (2001) [ 826] with 15% of the 1667 self-reported nut allergic registrants reporting almond allergy. In a later self-reported survey, Sicherer et al. (2003) [ 736] report that almond is the third most common tree nut to cause allergy in the USA after walnut and cashew with 32/82 responders reporting allergy. In these patients almond allergy is the consequence of cross-reactivity (similarity) between pollen allergens and similar proteins in vegetable foods. As such proteins are rapidly destroyed in the stomach this kind of food allergy is generally mild: in most cases oral allergy syndrome is the only allergic symptom. Moreover, these patients tolerate heat-processed almonds because allergens are heat-labile. Bargman et al. (1992) [734] report found that 7/8 patients showed diverse IgE specificity and one (RAST ratio 2.1) did not bind the extract. Binding to a 45-50 kDa protein or group of proteins was frequent and binding to 70 kDa fell after blanching. Pasini et al. (2000) [ 728] found positive SPT for all 5 atopic patients although only 2 had clinical symptoms with almond. Allergen properties & biological function: Amandin is the major almond storage protein and is one of the legumin family of 11S seed storage globulins.

Protocol: (controls, definition of positive etc) Clark and Ewan (2003) [ 615] used a positive (histamine 10 mg/mL) and negative control (saline). SPT wheal diameters were listed as <3 mm, 3-7 mm and >8 mm. Today, Friday, Allergy UK - the leading national patient charity for people living with all types of allergy - also issued an alert over the products following a number of calls to its helpline from concerned parents. Johansson SG, Hourihane JO, Bousquet J, Bruijnzeel-Koomen C, Dreborg S, Haahtela T, Kowalski ML, Mygind N, Ring J, van Cauwenberge P, van Hage-Hamsten M, Wuthrich B; EAACI (the European Academy of Allergology and Cinical Immunology) nomenclature task force.Process, chemical, enzymatic: Venkatachalam et al. (2002) [ 726] show that binding to rabbit monoclonal antibodies and to human IgE partially survives roasting, blanching, autoclaving, and microwave heating. Binding to the 39 kDa to 66 kDa bands is more stable than to the lower Mr. bands. A revised nomenclature for allergy. An EAACI position statement from the EAACI nomenclature task force. Production and characterization of rabbit polyclonal antibodies to almond (Prunus dulcis L.) major storage protein. Almond, hazelnut, Walnut, Cashew, Pecan nut, Brazil nut, Pistachio nut, Macadamia nut Queensland nut, Mustard and Sesame seeds There is also a milder form of tree nut allergy which is associated with birch pollen allergy, where symptoms are confined largely to the mouth, causing a condition called “oral allergy syndrome” (OAS). This condition is triggered by molecules found in tree nuts which are very similar to pollen allergens like the major birch pollen allergen called Bet v 1. These molecules tend to be destroyed by cooking, which can reduce the allergenicity of nuts and seeds for these allergic consumers.

Tree nuts are considered as one of the most frequent causes of food allergy, but almond allergy seems rather unusual. No good data for occurrence of almond allergy are available. In the United States and in the United Kingdom the frequency of tree nut allergy as a whole is estimated to range between 0.2% and 0.5% both in children and in adults. Tree nuts allergies appear early in childhood, but in Mediterranean countries sensitization to heat-resistant proteins may appear in adults. It is presently unknown whether allergic patients may become tolerant after some years of avoidance. Reactions to nuts and seeds can also occur as a consequence of hidden nut ingredients or traces of nuts and certain seeds introduced as a consequence of food handling or manufacturing. As a result tree nuts and seeds have been included in Annex IIIa of the EU food labelling directive. The following (including products thereof) must be declared on a label if they have been deliberately included in a food: Sathe et al. (2001) [ 730] found that the combined sera bound to proteins in the 39-66 kDa range and to a protein at about 16 kDa. Roux et al. (1999) [731] report binding to 66, 55, 50, 39-44, 37, 28, 17 and 10 kDa with different patterns for severe and mild symptoms. 12/14 subjects with life-threatening reactions to almonds showed IgE binding to almond extract and 11/14 to almond major protein (AMP). Sera from 6/11 patients with milder symptoms gave IgE binding to the 66 or 50 kDa allergens. 2/11 did not show IgE binding.

References (14)

Bargman et al. (1992) [734] report RAST against almond for 7/8 sera. Ratios were 2.1-59.8 times controls. Roux et al. (2003) [ 694] note that >50% of patients with serious symptoms bind amandin and that the 66 kDa band corresponds to unprocessed amandin. Sathe et al. (2001) [ 730] transferred proteins onto nitrocellulose membranes which were incubated with pooled sera from five patients (diluted 1:5). Almond proteins bound by serum IgE were detected using equine polyclonal 125I-anti-human IgE (Sanofi Diagnostics Pasteur, Chaska, MN). Almond may be present as a “hidden allergen” in commercial food preparations; a case of almond-induced anaphylaxis due to the ingestion of curry is described. Due to possible cross-reactivity, almond-allergic patients should avoid other tree nuts, such as hazelnut and Brazil nuts, unless their good tolerance has been clearly proven by reliable tests.