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

Evid Based Complement Alternat Med

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

Published: September 2016

AI Article Synopsis

  • The study focuses on quantifying apisin, a key protein in royal jelly, using HPLC, a common analytical technique.
  • Purification methods like isoelectric precipitation and size-exclusion chromatography confirmed the presence of apisin through SDS-PAGE and LC-MS analyses.
  • The research establishes a standardized method for measuring apisin, revealing its consistent content in natural royal jelly, which can serve as a reference for assessing the quality of royal jelly in future studies.

Article 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.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5045987PMC
http://dx.doi.org/10.1155/2016/5040528DOI Listing

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