Corpus ID: 44845506

Purification and complete amino acid sequence of a new type of sweet protein taste-modifying activity, curculin.

  title={Purification and complete amino acid sequence of a new type of sweet protein taste-modifying activity, curculin.},
  author={Hideyuki Yamashita and S Theerasilp and Toshihiro Aiuchi and Kazuyasu Nakaya and Y. Nakamura and Yoshie Kurihara},
  journal={The Journal of biological chemistry},
  volume={265 26},
A new taste-modifying protein named curculin was extracted with 0.5 M NaCl from the fruits of Curculigo latifolia and purified by ammonium sulfate fractionation, CM-Sepharose ion-exchange chromatography, and gel filtration. Purified curculin thus obtained gave a single band having a Mr of 12,000 on sodium dodecyl sulfate-polyacrylamide gel electrophoresis in the presence of 8 M urea. The molecular weight determined by low-angle laser light scattering was 27,800. These results suggest that… Expand
Purification, complete amino acid sequence and structural characterization of the heat-stable sweet protein, mabinlin II.
High similarity was found between the amino acid sequences of mabinlin II and 2S seed storage proteins, especially 2S albumin AT2S3 in Arabidopsis thaliana (mouse-ear cress). Expand
Molecular cloning of curculin, a novel taste-modifying protein with a sweet taste.
Northern blot analysis showed that the mRNA for curculin was first detected in Curculigo latifolia fruits at 2 weeks after pollination and remained at a constant level for the following 4 weeks. Expand
Curculin Exhibits Sweet-tasting and Taste-modifying Activities through Its Distinct Molecular Surfaces*
These findings suggest that the two activities of the curculin heterodimer are expressed through its two different modes of interactions with the T1R2-T1R3 heterodimmeric sweet taste receptor. Expand
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The hypothesis that neoculin is in dynamic equilibrium between open and closed states, and that the addition of an acid shifts the equilibrium to the open state, allowing ligand-receptor interaction is proposed. Expand
Characteristics of antisweet substances, sweet proteins, and sweetness-inducing proteins.
  • Y. Kurihara
  • Chemistry, Medicine
  • Critical reviews in food science and nutrition
  • 1992
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Neoculin as a New Taste-modifying Protein Occurring in the Fruit of Curculigo latifolia
A new taste-modifying protein, named neoculin, is found of the same origin as curculin, and is characterized as a heterodimeric protein consisting of an acidic, glycosylated subunit of 113 amino acid residues and a basic subunit that is the monomericCurculin itself. Expand
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The original sweetness and taste-modifying activity of rNCL were comparable to those of native NCL when confirmed by calcium imaging with human embryonic kidney cells expressing the human sweet taste receptor and by sensory tests. Expand