Abstract
Ten overlapping peptides (20 amino acids in length with an offset of 10 amino acids) spanning the amino acid sequence of Pacific mackerel, Scomber japonicus parvalbumin (Sco j 1), were synthesized and evaluated for IgE-binding ability by fluorescence ELISA using fish-allergic patient sera. As a result, the region 21–40 was judged to contain a major IgE epitope of Sco j 1. However, this region was not necessarily assumed to be a major IgE epitope for the parvalbumins from seven other species of fish (sardine, Japanese eel, cod, horse mackerel, crimson sea bream, skipjack and flounder). Ala-scanning experiments revealed that eight amino acid residues (Ser-23, His-26, Lys-27, Lys-28, Lys-31, Cys-33, Leu-35 and Lys-38) are important for the IgE-binding of Sco j 1. Some of these residues are replaced by different residues in the parvalbumins of the other seven species of fish.
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