Determination of royal jelly freshness by ELISA with a highly specific anti-apalbumin 1, major royal jelly protein 1 antibody

Shen, Lirong; Wang, Yiran; Zhai, Liang; Zhou, Wen-Xiu; Tan, Liang-liang; Li, Meilu; Liu, Dandan; Xiao, Fa

doi:10.1631/jzus.b1400223

Cited by 21 publications

(24 citation statements)

References 42 publications

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“…Therefore, we predict that the apisin content can be used as an RJ quality standard. Several researchers have reported an enzyme-linked immunosorbent assay (ELISA) method for quantifying apisin [ 14 – 16 ]. However, the ELISA method directly measures only the amount of MRJP1, not apisin itself.…”

Section: Introductionmentioning

confidence: 99%

Quantitative Analysis of Apisin, a Major Protein Unique to Royal Jelly

Furusawa

Arai

Kato

et al. 2016

Evidence-Based Complementary and Alternative Medicine

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Apisin, a protein that is unique to royal jelly (RJ), is known to compose the greater part of the RJ proteins and to exist as a heterooligomer containing major royal jelly protein 1 and apisimin. However, few reports on the methods for quantifying apisin have been published. Thus, we attempted to quantify apisin using HPLC, a widely used analytical technique, as described below. Isoelectric precipitation and size-exclusion chromatography were used to obtain the purified protein, which was identified as apisin by SDS-PAGE and LC-MS analyses. The purified apisin was lyophilized and then used to generate a calibration curve to quantify apisin in RJ. The apisin content was fairly constant (i.e., 3.93 to 4.67 w/w%) in natural RJ. This study is the first to describe a simple, standardized method for quantifying apisin using HPLC and suggests that apisin can be used as a benchmark for future evaluations of RJ quality.

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Section: Introductionmentioning

confidence: 99%

Quantitative Analysis of Apisin, a Major Protein Unique to Royal Jelly

Furusawa

Arai

Kato

et al. 2016

Evidence-Based Complementary and Alternative Medicine

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“…SDS-PAGE analysis of MRJPs showed four main protein bands ranging from 49 to 77 kDa in molecular weight, which are identified as MRJP5, MRJP3, MRJP1, and MRJP2, respectively (Fig. 1) according to the previous work (Shen et al, 2015).…”

Section: Composition Of Mrjpsmentioning

confidence: 55%

Evaluation of the major royal jelly proteins as an alternative to fetal bovine serum in culturing human cell lines

Chen

Xin

Qian

et al. 2016

J. Zhejiang Univ. Sci. B

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Royal jelly (RJ) is a well-known bioactive substance. It contains large amounts of major royal jelly proteins (MRJPs), which express growth-factor-like activity in several animal and human cell lines. However, the question on whether MRJPs possess growth-factor-like activity on all types of cell cultures remains. In order to determine whether MRJPs can be used as an alternative to fetal bovine serum (FBS) in different types of human cell culture, the proliferation of the complex serum with different ratios of MRJPs/FBS (M/F) was evaluated on five cell lines: 293T, HFL-I, 231, HCT116, and Changliver using MTT (3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide) assay. The proliferation activity of the combination of the complex M/F serum with cytokines on the test cell lines was also measured. The results demonstrated that the complex serum with M/F 6/4 possessed the highest proliferation activity similar to or in excess of FBS. However, no activity of complex medium with M/F 6/4 was observed in 231 cells, indicating a selectivity of MRJPs on cell types. Compared with the complex medium with M/F 6/4, the complex medium with M/F 6/4 together with two cytokines, epidermal growth factor (EGF) and insulin-transferrin-selenium (ITS), promoted proliferations of Changliver, 293T, HCT116, and HFL-I by 18.73%-56.19% (P<0.01). Our findings demonstrate that MRJPs could partially replace FBS in culturing many human cell lines.

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“…Then, the protein was separated and confirmation using the SDS‐PAGE technique and followed by western blot technique (targeting MRJP1) by the method described previously by Shen et al. (2015) to confirm the presence of MRJP1 in RJ.…”

Section: Methodsmentioning

confidence: 99%

“…As aforementioned the protein levels of EGCG‐RJ protein complex were estimated and separated using the SDS‐PAGE technique (12% polyacrylamide gel) and followed by western blot technique (targeting MRJP1‐using primary polyclonal antibody at 1:1,000 dilution bought from MYBioSource Inc., MA, USA) to confirmed the presence of MRJP1 in EGCG‐RJ protein complex as indicated by Shen et al. (2015).…”

Section: Methodsmentioning

confidence: 99%

Improved bioavailability of EGCG after complexation with royal jelly protein

Han

Chiu

et al. 2020

J Food Biochem

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This study was designed to check whether complexation of royal jelly (RJ) proteins with green tea extract enriched with EGCG, would enhance the bioavailability on C2BBe1 cells. The total phenolic and EGCG of green tea extract (GTex) as well as the protein level of RJ were measured. The best entrapment efficiency (30.47%) was noted at a 10:4 ratio (RJ:EGCG of GTex) to confirm the maximum EGCG‐RJ complexation. Followed by in vitro studies to check the cytotoxicity, morphological changes, EGCG uptake, and TBARS (antioxidant) activity were evaluated on C2BBe1 cells. The EGCG‐RJ protein complex showed less toxicity without any morphological changes with better cellular EGCG uptake than GTex or GTex‐RJ mixture on CeBBe1 cells. Besides, the EGCG‐RJ protein complex display maximum TBARS suppressing activity to showcase better stability. This study infers that complexation of RJ proteins with EGCG (EGCG‐RJ protein complex) could significantly improve the bioavailability of EGCG. Practical applications EGCG is the major active component of green tea, which is responsible for various biological functions. Previous studies have indicated that complexation of EGCG with proteins (act as a carrier) could considerably improve the bioavailability of EGCG. Hence, the author speculates that complexation or combination of RJ with green tea (EGCG), might improve the bioavailability as well as enhance its biological properties. The outcome of this cell line study showed that the EGCG‐RJ protein complex showed better bioavailability than EGCG or GTex, and thus, indicating that this novel complex can be used in the future for better EGCG bioavailability with improved biological function. However, further studies are needed to confirm the types of interaction and the reason for better bioavailability.

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Determination of royal jelly freshness by ELISA with a highly specific anti-apalbumin 1, major royal jelly protein 1 antibody

Cited by 21 publications

References 42 publications

Quantitative Analysis of Apisin, a Major Protein Unique to Royal Jelly

Quantitative Analysis of Apisin, a Major Protein Unique to Royal Jelly

Evaluation of the major royal jelly proteins as an alternative to fetal bovine serum in culturing human cell lines

Improved bioavailability of EGCG after complexation with royal jelly protein

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