An enzyme immunoassay and immunoblot analysis for curculin, a new type of taste-modifying protein: cross-reactivity of curculin and miraculin to both antibodies.
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.
Nakajo
S
S
Laboratory of Biological Chemistry, School of Pharmaceutical Sciences, Showa University, Tokyo, Japan.
Akabane
T
T
Nakaya
K
K
Nakamura
Y
Y
Kurihara
Y
Y
D003429:Cross Reactions; D006023:Glycoproteins / Q000276:immunology; D007118:Immunoassay; D007124:Immunoenzyme Techniques; D010940:Plant Proteins / Q000032:analysis* / Q000276:immunology; D010944:Plants / Q000737:chemistry*; D013549:Sweetening Agents / Q000032:analysis*
D006023:Glycoproteins; D010940:Plant Proteins; D013549:Sweetening Agents; C065630:curculin; C008533:miraculin protein, Synsepalum dulcificum; C002541:monellin protein, Dioscoreophyllum cumminsii; C003427:thaumatin protein, plant