Open AccessLocalization of Antigenic Determinants on Bovine Encephalitogenic Protein
Author(s) -
Bergstrand Håkan
Publication year - 1972
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1972.tb01818.x
Subject(s) - peptide , proteolysis , antigen , tryptophan , in vitro , chemistry , epitope , biochemistry , residue (chemistry) , peptide sequence , amino acid , microbiology and biotechnology , biology , immunology , gene , enzyme
By peptic or tryptic proteolysis of different fragments of bovine encephalitogenic protein, a set of small fragments covering the following regions of the native protein have been obtained: 44–68, 44–89, 75–91, 93–116, 114–130, 134–150, and 154–170 (the amino acid residues are numbered according to [1]). These fragments were used in the macrophage migration inhibition technique in guinea pigs (an assay which is vividly considered as a correlate in vitro to delayed type hypersensitivity) to study the localization of antigenic determinants in the protein. The results indicate the presence of at least one determinant in each of regions 44–68, 134–140, and 154–170. Furthermore, the rather strong determinant, which has previously been localized around the single tryptophan residue in the protein does not seem to be contained within peptide 114–130, as this peptide is considered unreactive in the assay. On the other hand, this peptide shows full encephalitogenic activity.