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Complete amino acid sequence and structure characterization of the taste-modifying protein, miraculin.
Theerasilp S, Hitotsuya H, Nakajo S, Nakaya K, Nakamura Y, Kurihara Y. Theerasilp S, et al. Among authors: kurihara y. J Biol Chem. 1989 Apr 25;264(12):6655-9. J Biol Chem. 1989. PMID: 2708331 Free article.
The complete amino acid sequence of miraculin purified from miracle fruits by a newly developed method (Theerasilp, S., and Kurihara, Y. (1988) J. Biol. Chem. 263, 11536-11539) was determined by an automatic Edman degradation method. ...
The complete amino acid sequence of miraculin purified from miracle fruits by a newly developed method (Theerasilp, S., and Kurihara, …
Structures of heat-stable and unstable homologues of the sweet protein mabinlin. The difference in the heat stability is due to replacement of a single amino acid residue.
Nirasawa S, Nishino T, Katahira M, Uesugi S, Hu Z, Kurihara Y. Nirasawa S, et al. Among authors: kurihara y. Eur J Biochem. 1994 Aug 1;223(3):989-95. doi: 10.1111/j.1432-1033.1994.tb19077.x. Eur J Biochem. 1994. PMID: 8055976 Free article.
In previous studies, we purified the heat-stable analogue, mabinlin II, from the seeds of Capparis masaikai Levl. and determined its amino acid sequence [Liu, X., Maeda, S., Hu, Z., Aiuchi, T., Nakaya, K. & Kurihara, Y. (1993) Eur. J. Biochem. 211, 281-287] and …
In previous studies, we purified the heat-stable analogue, mabinlin II, from the seeds of Capparis masaikai Levl. and determined its amino a …
893 results