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N‐terminal amino acid sequence of a major allergen of Japanese cedar pollen ( Cry j I)
Author(s) -
Taniai Madoka,
Ando Shunsaku,
Usui Mitsuko,
Kurimoto Masashi,
Sakaguchi Masahiro,
Inouye Sakae,
Matuhasi Tyoku
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80945-1
Subject(s) - allergen , amino acid , peptide sequence , monoclonal antibody , pollen , sequence (biology) , peptide , antibody , chemistry , biochemistry , biology , microbiology and biotechnology , immunology , botany , allergy , gene
A purified preparation of a major allergen of Japanese cedar pollen, sugi basic protein (SBP, Cry j I), was separated into 5 subtractions of 50‐45 kDa. All of the SBP subtractions were confirmed to be reactive to IgE antibodies from patients with Japanese cedar pollinosis, and also to mouse anti‐SBP monoclonal antibodies. The sequences of 20 N‐terminal amino acids of these 5 subtractions were found to be identical. Peptide mapping analyses of the SBP subtractions showed similar patterns, with some differences which might in part be due to the existence of an N ‐linked carbohydrate chain. The N‐terminal amino acid sequence of SBP was identical to the reported sequence of an allergen of mountain cedar which vegetated in North America.

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