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Primary structure and allergenic activity of trypsin inhibitors from the seeds of buckwheat ( Fagopyrum esculentum Moench)
Author(s) -
Park Sung-Soo,
Abe Kei,
Kimura Makoto,
Urisu Atsuo,
Yamasaki Nobuyuki
Publication year - 1997
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/s0014-5793(96)01367-1
Subject(s) - fagopyrum , trypsin , chemistry , botany , primary (astronomy) , biology , biochemistry , enzyme , physics , astronomy
The complete amino acid sequences of two trypsin inhibitors BWI‐2a and BWI‐2b from the seeds of buckwheat ( Fagopyrum esculentum Moench) were determined. BWI‐2b consists of 51 amino acid residues containing two disulfide bonds. BWI‐2a shares all amino acids with BWI‐2b except for the C‐terminal tripeptide: BWI‐2a lacks Glu‐Gly‐Asn and ends with the Asp residue, making a total of 48 residues in the chain. The two disulfide bonds connect Cys 11 to Cys 32 and Cys 15 to Cys 28 . BWI‐2b shows no relatedness to the other buckwheat trypsin inhibitor reported [Belozersky et al. (1995) FEBS Lett. 371, 264–266]. Sequence comparison of BWI‐2b with those of the other proteins included in PIR showed that BWI‐2b is significantly homologous to the N‐terminal region of storage proteins classified in the vicilin family. Furthermore, the allergenic activity of BWI‐2b and the other buckwheat trypsin inhibitor BWI‐1 was examined using the radioallergosorbent test. The result indicated that both inhibitors BWI‐2b and BWI‐1 have IgE binding activity, albeit to a low extent, suggesting that they might be minor allergenic proteins in buckwheat seeds.