Changes of structure and IgE binding capacity of shrimp (Metapenaeus ensis) tropomyosin followed by acrolein treatment
Author:
Affiliation:
1. College of Food Science and Engineering
2. Ocean University of China
3. Qingdao
4. P.R. China
5. Qingdao Municipal Hospital
Abstract
The changes of structure and IgE binding capacity of shrimp tropomyosin following acrolein treatment are explored at the molecular level.
Funder
National Natural Science Foundation of China
Publisher
Royal Society of Chemistry (RSC)
Subject
General Medicine,Food Science
Link
http://pubs.rsc.org/en/content/articlepdf/2017/FO/C6FO01479H
Reference36 articles.
1. Induction of Redox Instability of Bovine Myoglobin by Adduction with 4-Hydroxy-2-nonenal
2. Cloning, expression, and primary structure of tropomyosin, the major heat-stable shrimp allergen
3. Correlation of specific IgE to shrimp with cockroach and dust mite exposure and sensitization in an inner-city population
4. Effects of combined high pressure and thermal treatments on the allergenic potential of shrimp (Litopenaeus vannamei) tropomyosin in a mouse model of allergy
5. Effects of food processing on the stability of food allergens
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