Towards royal jelly proteome

Abstract

The recent availability of the honey-bee Apis mellifera genome and trascriptome of both the female castes, has stimulated new efforts in investigating the protein composition of royal jelly (RJ), its role in caste differentiation and its quality and typicality by a proteomic approach. This study is aimed both to separate and identify proteins of royal jelly and to detect some of them in honey-bee pollen-bread by using two-dimensional gel electrophoresis, mass spectrometry and by de novo sequencing. All the identified proteins belonged to the Apis mellifera genome. Apalbumin 1 was also confirmed to be present in honey-bee pollen-bread where the presence of apalbumin 2 was also found. In addition several fragments of apalbumin 1 and apalbumin 3 were also found in RJ. These could be the result of protease activity other than that of serine-protease. This study is a contribution to the description of royal jelly proteome.

The immunostimulatory effect of the recombinant apalbumin 1–major honeybee royal jelly protein–on TNFα release

“…We assume that recombinant protein fragments do not contain specific sequences, which are necessary for proteolytic degradation by a complex of proteases from E. coli, particularly trypsin-like proteases. Moreover, the degradation of native monomeric, but not oligomeric, form of Apa1 in RJ was also observed [19,[42][43][44]. It has been recently indicated that Apa1 in RJ is specifically degraded by unknown metalloproteinase(s), which seem to have restricted substrate specificity [43].…”

Bioactive compounds and health-promoting properties of royal jelly: A review

“…Several studies have analysed MRJPs by reducing SDS-PAGE, including 2-DE Sano et al, 2004;Santos et al, 2005;Scarselli et al, 2005;Schmitzova et al, 1998;Schonleben et al, 2007). Separated bands on SDS-PAGE do not reflect the data for intact proteins, as samples are boiled and reduced as part of the standard Laemmli (1970) method.…”

Identification of the distribution of adenosine phosphates, nucleosides and nucleobases in royal jelly

“…Perchloric acid is the commonly used agent to extract ATP-related compounds from intact cells due to its strong acidic nature, and it can precipitate protein effectively (Coolen et al, 2008;Fukuuchi et al, 2013). RJ is a complex matrix containing several proteins (Scarselli et al, 2005) which needs to be removed before analysis. Use of higher concentration of ethanol, acetone or perchloric acid helps to precipitate the protein effectively from the RJ samples (Zhou et al, 2007).…”