A quantitative enzyme immunoassay for miraculin in Richadella dulcifica (miracle fruit)
- 1 November 1988
- journal article
- research article
- Published by Oxford University Press (OUP) in Chemical Senses
- Vol. 13 (4) , 663-669
- https://doi.org/10.1093/chemse/13.4.663
Abstract
We have developed an enzyme-linked immunoabsorbent assay for miraculin, a glycoprotein which is capable of modifying sour taste into sweet. Antiserum against purified miraculin was raised in rabbits and the anti-miraculin in IgG was purified using a Protein A-Cellulofine column and then conjugated with horseradish peroxidase. The established enzyme immunoassay method was able to accurately quantitate pg amounts of miraculin in crude extracts of miracle fruit. The amounts of miraculin in miracle fruit increased dramatically seven weeks after pollination and at eight weeks reached 102 μg/mg protein in the fruit.This publication has 4 references indexed in Scilit:
- Complete purification and characterization of the taste-modifying protein, miraculin, from miracle fruit.Journal of Biological Chemistry, 1988
- Isolation and chemical properties of multiple active principles from miracle fruitBiochimica et Biophysica Acta (BBA) - General Subjects, 1982
- “Western Blotting”: Electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein AAnalytical Biochemistry, 1981
- A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye BindingAnalytical Biochemistry, 1976