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A major epitope of synthetic rabbit encephalitogen S24 disclosed through the use of a tritiated peptide probe
Author(s) -
Tyrey S. J.,
Potter N. T.,
Day E. D.,
Hashim G. A.
Publication year - 1987
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/jnr.490180317
Subject(s) - epitope , peptide , tritium , chemistry , chromatography , high performance liquid chromatography , labelling , antibody , biochemistry , biology , physics , nuclear physics , immunology
The antibody recognition of synthetic rabbit encephalitogen S24 (TTHYGSLPQKG), which had been inactivated by extensive iodination, was fully restored by tritium‐iodine exchange during boron hydride reduction. A highly active form of 3 H‐S24 was obtained by reverse‐phase high‐performance liquid chromatography (HPLC) purification of the crude product and could be further separted into three continuous subfractions, the latter two of which were fully active from an immunochemical point of view. A major epitope was diclosed through use of the 3 H‐S24 probe, which required the intact S24 peptide for its expression. Confirmation of two linear epitopes previously encountered, GSLPQK and THYGSL, was also obtained, the latter through the use of the third HPLC subfraction of 3 H‐S24.