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

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.

SUBMITTER: Furusawa T

PROVIDER: S-EPMC5045987 | biostudies-other | 2016

REPOSITORIES: biostudies-other

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

Furusawa Takako T Arai Yasuko Y Kato Kenji K Ichihara Kenji K

Evidence-based complementary and alternative medicine : eCAM 20160918

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 identi ...[more]

PMID: 27721892

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