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- W2019774582 abstract "In the early stage of ripening of cherry-tomato fruits (Lycopersicon esculentum var. cherry), the lectin activity increased logarithmically and reached a plateau at day 10 after flowering. During purification of lectin from ripe and unripe fruits, a 42-kDa protein was found abundantly in unripe fruits. The protein cross-reacted with anti-cherry-tomato-lectin serum, retained chitin-binding ability, but showed no lectin activity. Comparative studies between the structure of the lectin and the 42-kDa protein were done. N-Terminal amino acid sequences of the lectin, peptides derived from the S-pyridylethylated lectin, and fragments generated by limited proteolysis of the native lectin showed that the lectin was comprised of three domains, Hyp-rich, Cys-rich, and Gln-rich, and the alignment of them was as this order from the N-terminus. Studies on the 42-kDa protein showed that it contained two of the three domains, Cys-rich and Gln-rich, but the amino acid sequence analysis showed that the protein should be a product of another gene." @default.
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- W2019774582 date "2001-01-01" @default.
- W2019774582 modified "2023-10-11" @default.
- W2019774582 title "Domain Construction of Cherry-tomato Lectin: Relation to Newly Found 42-kDa Protein" @default.
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- W2019774582 doi "https://doi.org/10.1271/bbb.65.86" @default.
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