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egg hypersensitivity/protease

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AtikEsè klinikPatant
6 rezilta yo
METHODS Glycation of allergens via Maillard reaction or chemical conjugation has been shown to influence susceptibility to food-induced allergies. It is hypothesized that mucosal immune response bias can be favorably altered by orally administering various forms of glycated ovalbumin
Ovalbumin (OVA) is the most abundant egg white protein, but is also a major egg allergen. Desensitization of OVA may be a good way to control an egg allergy. In this study, caffeic acid-assisted cross-linked OVA catalyzed by polyphenol oxidase (PPO) was prepared, the effect of cross-linking on the

Attenuation of allergic immune response phenotype by mannosylated egg white in orally induced allergy in BALB/c mice.

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Food allergies are attributed to an imbalance in immune response to ubiquitous antigens. A previous study demonstrated that mannose glycation (mannosylation) of ovalbumin decreased allergenicity in vivo. The proposed research targets mannosylation of various common allergens that may help prevent

Dephosphorylation reduces passage of ovalbumin antigen through intestinal epithelial Caco-2 cell monolayers.

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Allergenic potential of food proteins is associated with stability to gastric and pancreatic digestive enzymes. However, much attention has not been focused on intracellular digestion of protein antigens during the passage through intestinal epithelia. We report here the degradation and survival of
The aim of the present study was to compare various glycated ovalbumin (OVA)-monosaccharides, including OVA-mannose (Man), -glucose, -ribose, and -fructose, in the attenuation of OVA-induced allergic response in a BALB/C mouse model and the potential mechanisms of immunological modulation. The
Successful prevention of food allergy requires the identification of the factors adversely affecting the capacity to develop oral tolerance to food antigen in early life.To determine whether oral exposure to Der p through breastmilk affects gut mucosal
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