A rapid method to isolate soluble royal jelly proteins |
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Authors: | Reo Nozaki Shogo Tamura Aimi Ito Takanori Moriyama Kikuji Yamaguchi Toru Kono |
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Affiliation: | 1. Division of Gastroenterologic and General Surgery, Department of Surgery, Asahikawa Medical University, Asahikawa, Japan;2. Japan Royal Jelly Research Laboratories, Japan Royal Jelly & Co., Miyagi, Japan;3. Division of Health Sciences, Graduate School of Health Sciences, Hokkaido University, Sapporo, Japan;4. Research Fellow of the Japan Society for the Promotion of Science, Tokyo, Japan;5. Medical Laboratory Science, Faculty of Health Sciences, Hokkaido University, Sapporo, Japan |
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Abstract: | Soluble royal jelly (RJ) proteins (SRJPs) include the major RJ protein (MRJP) family, which contribute to the physiological actions of RJ. Although SRJPs are prepared using conventional methods involving dialysis and centrifugation, dialysis is a time-consuming process. We have therefore developed a simple method to isolate SRJPs from RJ. This new method produces 20-fold higher levels of SRJPs than that of the conventional procedure; hence, the levels obtained by the new and existing methods were compared. A 1-h ultracentrifugation separated SRJPs in the supernatant into upper, middle and lower layers. Each layer was analyzed by size-exclusion HPLC, SDS–PAGE and 2-DE. The upper and middle layers contained MRJP2 (52 kDa) and MRJP3 (60–70 kDa), while the lower layer contained MRJP1 (290 kDa). In nature, MRJP1 is a monomer and/or oligomer. When the lower layer was analyzed by Superose 12 HPLC, MRJP1 was predominantly an oligomer. Our MRJP isolation method reduces the procedure time by using ultracentrifugation without dialysis to obtain SRJPs and produces layers containing MRJP1 oligomers, MRJP2 and MRJP3. |
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Keywords: | Royal jelly Ultracentrifugation Soluble royal jelly proteins MRJP1 oligomer HPLC |
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