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Monday, June 30, 2008
Study Identifies 52 Royal Jelly Proteins 

Comprehensive Royal Jelly (RJ) Proteomics Using One- and Two-Dimensional
Proteomics Platforms Reveals Novel RJ Proteins and Potential
Phospho/Glycoproteins
J. Proteome Res, June 26, 2008

Abstract: Royal jelly (RJ) is an exclusive food for queen honey bee
(Apis mellifera L.) that is synthesized and secreted by young worker
bees. RJ is also widely used in medical products, cosmetics, and as
health foods. However, little is known about RJ functionality and the
total protein components, although recent research is attempting to
unravel the RJ proteome.

We have embarked on a detailed investigation of the RJ proteome, using a
modified protein extraction protocol and two complementary proteomics
approaches, one- and two-dimensional gel electrophoresis (1-DGE and
2-DGE) in conjunction with tandem mass spectrometry...

As the RJ from 48 (or sometimes 72) is commercially used, we selected
the RJ sample at 48 h for detailed analysis with the first collection.
1-DGE identified 90 and 15 proteins from the first and second selection,
respectively; in total, 47 nonredundant proteins were identified. 2-DGE
identified 105 proteins comprising 14 nonredundant proteins.

In total, 52 nonredundant proteins were identified in this study, and
other than the major royal jelly protein family and some other
previously identified proteins, 42 novel proteins were identified... 

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