Abstract
Major royal jelly proteins (MRJPs) are deemed to the most characteristic and abundant constituents in royal jelly. The present paper establishes a sequential process to purify the natural MRJP 1–3 by three different chromatographic procedures. Five individual proteins were obtained, including MRJP 1 oligomer 1, MRJP 1 oligomer 2, MRJP 1 monomer, MRJP 2 and MRJP 3s (contain three MRJP 3 variants) with a purity of 89.88%, 67.79%, 99.92%, 99.41%, and 99.97%, respectively. This is the first report that MRJP 1 mainly possesses three oligomers: a 228 kDa MRJP 1 oligomer 1, a 408 kDa MRJP 1 oligomer 2 and a 639 kDa MRJP 1 oligomer 3. We infer that MRJP 1 oligomer 3 (639 kDa) may be assembled by MRJP 1 oligomer 1 (228 kDa) and MRJP 1 oligomer 2 (408 kDa). The secondary structure of the purified MRJP 1–3 consisted predominantly of β-sheets and random coil in the native conformation. Our results will contribute to the physiological and physicochemical function of the purified individual MRJPs.
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