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Nucleotide sequence of a cDNA clone encoding a major allergenic protein in rice seeds Homology of the deduced amino acid sequence with members of α‐amylase/trypsin inhibitor family
Author(s) -
Izumi Hidehiko,
Adachi Takahiro,
Fujii Noboru,
Matsuda Tsukasa,
Nakamura Ryo,
Tanaka Kunisuke,
Urisu Atsuo,
Kurosawa Yoshikazu
Publication year - 1992
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(92)80443-k
Subject(s) - complementary dna , peptide sequence , cdna library , nucleic acid sequence , open reading frame , biology , biochemistry , amino acid , trypsin inhibitor , signal peptide , residue (chemistry) , microbiology and biotechnology , trypsin , enzyme , gene
A cDNA clone of rice major allergenic protein (RAP) was isolated from a cDNA library of maturing rice seeds. The cDNA had an open reading frame (486 nucleotides) which coded a 162 amino acid residue polypeptide comprising a 27‐residue signal peptide and a 135‐residue mature protein of M r 14,764. The deduced amino acid sequence of RAP showed a considerable similarity to barley trypsin inhibitor [1983, J. Biol. Chem. 258, 7998–8003] and wheat α‐amylase inhibitor [1981, Phytochemistry 20, 1781–1784].