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Evidence-Based Complementary and Alternative Medicine
Volume 2016 (2016), Article ID 5040528, 9 pages
http://dx.doi.org/10.1155/2016/5040528
Research Article

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

Nagaragawa Research Center, API Co., Ltd., 692-3 Nagara, Gifu 502-0071, Japan

Received 6 May 2016; Revised 11 July 2016; Accepted 27 July 2016

Academic Editor: Vassya Bankova

Copyright © 2016 Takako Furusawa et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

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.