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：6
期号：106
页码：41-45
出版社：Moldova State University
摘要：The final product of trypsin limited proteolysis of a subunit of storage 11S globulin from peanut seeds Ara h3(pdb|3c3v) consists of the intact 円-chain and 冄-chain fragments K and N. The fragment K disulfide bonded with the円-chain corresponds to the N-terminal half of the 円-barrel (Ile1-Arg109), and the fragment N corresponds to the adjacentC-terminal half (Lys110-Arg213). Identification of the respective 冄-chain cleavage points is based on the results ofelectrophoresis, the molecular mass of the residual protein determined using two independent methods, and on theanalysis of the level of accessibility of amino acid residues in a model structure of Ara h3 hexamer molecule. Thedestruction of the 冄-chain C-terminal region occurs in the course of formation of the fragments K and N. This regioncontains three of the four antigen determinants (IgE epitopes) identified in Ara h3. Thus, it seems likely that trypsinlimited proteolysis can essentially decrease the allergenicity level of the peanut 11S globulin.
