Literature DB >> 1737052

An enzyme immunoassay and immunoblot analysis for curculin, a new type of taste-modifying protein: cross-reactivity of curculin and miraculin to both antibodies.

S Nakajo1, T Akabane, K Nakaya, Y Nakamura, Y Kurihara.   

Abstract

We have developed an enzyme immunoassay method for curculin, a new type of taste-modifying protein. This method can accurately quantify 0.05-20 ng of curculin, a sensitivity about 3000-times that of the psychometric method. The content of curculin in the fruit of Curculigo latifolia increased gradually until 3 weeks after artificial pollination and dramatically at 4 weeks, to finally reach 1.3 mg per fruit. Immunoblot analysis indicated that antiserum to curculin was faintly reactive with miraculin, but not with thaumatin or monellin.

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Year:  1992        PMID: 1737052     DOI: 10.1016/0167-4838(92)90287-n

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  3 in total

1.  Curculin, a sweet-tasting and taste-modifying protein, is a non-functional mannose-binding lectin.

Authors:  A Barre; E J Van Damme; W J Peumans; P Rougé
Journal:  Plant Mol Biol       Date:  1997-03       Impact factor: 4.076

2.  De novo transcriptome analysis and comparative expression profiling of genes associated with the taste-modifying protein neoculin in Curculigo latifolia and Curculigo capitulata fruits.

Authors:  Satoshi Okubo; Kaede Terauchi; Shinji Okada; Yoshikazu Saito; Takao Yamaura; Takumi Misaka; Ken-Ichiro Nakajima; Keiko Abe; Tomiko Asakura
Journal:  BMC Genomics       Date:  2021-05-13       Impact factor: 3.969

3.  An efficient in vitro plantlet regeneration from shoot tip cultures of Curculigo latifolia, a medicinal plant.

Authors:  Nahid Babaei; Nur Ashikin Psyquay Abdullah; Ghizan Saleh; Thohirah Lee Abdullah
Journal:  ScientificWorldJournal       Date:  2014-02-27
  3 in total

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