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carya laciniosa/hypersensitivity
Veza se sprema u međuspremnik
5 rezultatima
RNA-Seq Analysis of Developing Pecan (Carya illinoinensis) Embryos Reveals Parallel Expression Patterns among Allergen and Lipid Metabolism Genes.
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The pecan nut is a nutrient-rich part of a healthy diet full of beneficial fatty acids and antioxidants, but can also cause allergic reactions in people suffering from food allergy to the nuts. The transcriptome of a developing pecan nut was characterized to identify the gene expression occurring
Airborne pollen of Carya, Celtis, Cupressus, Fraxinus and Pinus in the metropolitan area of Monterrey Nuevo Leon, Mexico.
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The concentration of pollen grains in the atmosphere over the metropolitan area of Monterrey, Nuevo Leon, Mexico, was analyzed throughout a year from March 2003-February 2004, focused on the genus Carya, Celtis, Cupressus, Fraxinus and Pinus owing to their interest as etiological pollinosis agents
Expression, purification and crystallization of pecan (Carya illinoinensis) vicilin.
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Tree nuts are responsible for many cases of severe food allergies. The 7S seed storage protein vicilin has been identified as a food allergen in many kinds of tree nuts. The vicilin protein consists of an N-terminal low-complexity region with antimicrobial activity and a C-terminal domain that forms
Contact dermatitis following sustained exposure to pecans (Carya illinoensis): a case report.
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Type I hypersensitivity reactions following ingestion of peanuts and tree nuts are well characterized. Cutaneous hypersensitivity reactions are less well characterized, yet they remain the second most common reaction pattern to contact with or ingestion of such nuts. We present a case of a patient
Identification and Characterization of a New Pecan [Carya illinoinensis (Wangenh.) K. Koch] Allergen, Car i 2.
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The 7S vicilin and 11S legumin seed storage globulins belong to the cupin protein superfamily and are major food allergens in many foods from the "big eight" food allergen groups. Here, for the first time, pecan vicilin was found to be a food allergen. Western blot experiments revealed that 30% of
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