Immunochemical Approach to Detection of Adulteration in Honey: Physiologically Active Royal Jelly Protein Stimulating TNF-α Release Is a Regular Component of Honey
- 25 March 2004
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of Agricultural and Food Chemistry
- Vol. 52 (8) , 2154-2158
- https://doi.org/10.1021/jf034777y
Abstract
The presence of royal jelly (RJ) proteins in honey collected from nectars of different plants, origin, and regions and in honeybee‘s pollen was detected by Western-blot analysis using polyclonal antibodies raised against water-soluble RJ-proteins. The most abundant RJ-protein in honeybee products corresponded to a 55 kDa protein. The N-terminal amino acid sequence of 55 kDa protein was N−I−L−R−G−E. This sequence is identical to the apalbumin-1, the most abundant protein of RJ. Apalbumin-1 is a regular component of honeybee products and thus is a suitable marker tool for proving adulteration of honey by means of immunochemical detection. Its presence in all tested samples of honeys and honeybee pollen was confirmed also by Western-blot analysis using polyclonal antibodies raised against recombinant apalbumin-1. It has been found that major RJ-proteins, apalbumin-1, and apalbumin-2, stimulate mouse macrophages to release TNF-α, which demonstrates that physiologically active proteins of honey could be used for its biological valuation. Keywords: Honey; adulteration; major royal jelly protein; honeybee products; immunochemical analysis; TNF-α releaseKeywords
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