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Ara h 1 is a seed storage protein from Arachis hypogaea (peanuts). It is a heat stable 7S vicilin-like globulin [1] with a stable trimeric form [2] that comprises 12-16% of the total protein in peanut extracts. [3] Ara h 1 is known because sensitization to it was found in 95% of peanut-allergic patients from North America. In spite of this high ...
NMR analysis [3] has confirmed earlier predictions of the protein structure and site of the major T-cell epitope. [4] The Bet v 1 protein comprises 6 anti-parallel beta-strands and 3 alpha-helices. Four of the strands dominate the global fold, and 2 of the helices form a C-terminal amphipathic helical motif.
The levels of mushroom respiratory allergy are as high as 30 percent of those with allergic disorder, but it is believed to be less than 1 percent of food allergies. [ 34 ] [ 35 ] Heavy rainfall (which increases fungal spore release) is associated with increased hospital admissions of children with asthma. [ 36 ]
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In the United States, food allergy affects as many as 5% of infants less than three years of age [103] and 3% to 4% of adults. [104] [105] The prevalence of food allergies is rising. [106] [107] [108] Food allergies cause roughly 30,000 emergency room visits and 150 deaths per year. [109]
These protein classes are collectively referred to as "gluten". [4] The storage proteins in other grains, such as maize and rice (rice protein), are sometimes called gluten, but they do not cause harmful effects in people with celiac disease. [3] Bread produced from wheat grains contains gluten.
The CATH Protein Structure Classification database is a free, publicly available online resource that provides information on the evolutionary relationships of protein domains. It was created in the mid-1990s by Professor Christine Orengo and colleagues including Janet Thornton and David Jones , [ 2 ] and continues to be developed by the Orengo ...
PLTPs are pan-allergens, [11] [12] and may be directly responsible for cases of food allergy. Pru p 3, the major allergen from peach, is a 9-kDa allergen belonging to the family of lipid-transfer proteins. [13] Allergic properties are closely linked with high thermal stability and resistance to gastrointestinal proteolysis of the proteins. [14]