Wednesday, August 24, 2011

Study Identifies New Royal Jelly Proteins

Novel Royal Jelly Proteins Identified by Gel-based and Gel-Free Proteomics
J Agric Food Chem, 2011 Aug 22

Royal jelly (RJ) plays an important role in caste determination of honeybee (a genetically same female egg develops either into a queen or worker bee depending on the time and the amount of RJ feed to the larva) and also has numerous health promoting properties for humans.

We applied gel-based and gel-free proteomics approaches followed with high-performance liquid chromatography-chip quadruple time-of-flight tandem mass spectrometry to comprehensive reveal RJ proteome.

Generally, 37 and 22 nonredundant proteins were identified by one-dimensional gel electrophoresis and gel-free analysis, respectively, and 19 new proteins were found by these two proteomics approaches.

In agreement with previous studies, major royal jelly proteins was the main protein family in RJ and proteins related to carbohydrate metabolism as glucose oxidase, alpha-glucosidase precursor, glucose dehydrogenase, were also successfully identified. Importantly, the 19 newly identified proteins were mainly classified into three functional categories: oxidation-reduction, ergic53 CG6822-PA, isoform A isoform 1, Sec61 CG9539-PA and ADP/ATP translocase; protein binding, regucalcin (RC) and translationally controlled tumor protein CG4800-PA isoform 1 and lipid transport, apolipophorin-III-like protein.

These new findings not only significantly increase the RJ proteome coverage, but also help us get new knowledge of RJ for honeybee biology and potential use for human health promotion.

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