A major epitope of synthetic rabbit encephalitogen S24 disclosed through the use of a tritiated peptide probe.
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 3H-S24 was obtained by reverse-phase high-performance liquid chromatography (HPLC) purification of the crude product and could be further separated into three continuous subfractions, the latter two of which were fully active from an immunochemical point of view. A major epitope was disclosed through use of the 3H-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 3H-S24.
D000818:Animals; D000918:Antibody Specificity; D002851:Chromatography, High Pressure Liquid; D000939:Epitopes / Q000032:analysis*; D008968:Molecular Conformation; D004676:Myelin Basic Protein / Q000138:chemical synthesis* / Q000276:immunology; D010446:Peptide Fragments / Q000138:chemical synthesis* / Q000276:immunology; D011817:Rabbits; D011863:Radioimmunoassay; D011869:Radioligand Assay; D014316:Tritium
D000939:Epitopes; D004676:Myelin Basic Protein; D010446:Peptide Fragments; D014316:Tritium