期刊名称：Studia Universitatis Moldaviae: Stiinte Sociale
印刷版ISSN：1814-3199
电子版ISSN：2345-1017
出版年度：2017
卷号：1
期号：101
页码：37-40
出版社：Moldova State University
摘要：Papain proteolysis of the storage 11S globulin Ara h3 from peanut seeds starts from the detachment of an extended -chain C-terminal sequence covering the region of -helices. Further cleavage of a loop between -strands E’ and F’ inside the central part of -chain -barrel occurs generating fragments connected with intact -chains via a disulfide bond and those retained inside the molecule of partially hydrolyzed 11S globulin due to non-covalent interactions. In accordance with the described proteolysis scenario, the C-terminal -chain region containing three of the four antigen determinants (IgE epitopes) identified in the peanut 11S globulin is destroyed during the initial papain action. Therefore, the level of Ara h3 allergenicity can be decreased via papain limited proteolysis.
