免疫原性
医学
组织谷氨酰胺转胺酶
消化(炼金术)
谷胱甘肽
BETA(编程语言)
药理学
免疫学
生物化学
酶
抗体
色谱法
生物
化学
计算机科学
程序设计语言
作者
Milena Morandi Vuolo,Mariana Battaglin Villas-Boas,Flávia Maria Netto,Ricardo de Lima Zollner
标识
DOI:10.1097/01.wox.0000411812.63915.fd
摘要
Background
Among the milk whey proteins, β-lactoglobulin (β-Lg) is the main allergen. In native state, β-Lg is resistant to pepsin, which is considered an indicator of its allergenic potential. Protein antigenicity can be reduced by treatment with transglutaminase (TG), an enzyme which catalyses inter or intra crosslink between Lys and Gln residues. Reducing agents have been used to increase the access of TG to the Lys and Gln residues. This study aimed at investigating the antigenicity and digestibility by pepsin of β-Lg modified by TG in the presence of the reducing agent glutathione (GSH).
科研通智能强力驱动
Strongly Powered by AbleSci AI