2020/06/02 by Xueyu Wang, Jie Dong, Jiangtao Qiao +2 · 1 citation
Agricultural and Biological Sciences · Medicine · Pharmacology, Toxicology and Pharmaceutics · #Advancements in Transdermal Drug Delivery #Bee Products Chemical Analysis #Healthcare and Venom Research
paper · doi:10.1080/00218839.2020.1761071
crossref issued 2020/06/02 · crossref published 2020/06/02 · crossref published-online 2020/06/02 · openalex publication_date 2020/06/02 · crossref created 2020/06/02 · crossref published-print 2020/10/19 · crossref deposited 2021/05/28 · openalex created_date 2025/10/10 · crossref indexed 2026/07/28 · openalex updated_date 2026/07/29
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.