Identification and partial characterization of the major royal jelly protein of the honey bee (Apis melliferaL.)

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Abstract
SUMMARY The major royal jelly protein (MRJP) derived from the hypopharyngeal glands of the honey bee, Apis mellifera, was isolated by ionexchange chromatography. When using SDS-PAGE, the preparation exhibited only one band, which had a molecular mass of 57 kDa and consisted of at least eight components with similar isoelectric points with a range of pH 4.5—pH 5.0. Components of the MRJP were the most acidic proteins of royal jelly. The proteins from different parts of the honey bee body were analysed with antiserum raised against MRJP. Mobilities of proteins isolated directly from hypopharyngeal glands were greater than those of royal jelly proteins. The most significant difference was in the major protein. The MRJP and the major protein from hypopharyngeal glands had apparent molecular masses of 57 kDa and 55 kDa respectively. This difference reflects some modification of hypopharyngeal gland proteins.