Abstract:

This study evaluated the structure characteristics and anti-motor fatigue activity of selenium-containing protein
purified from Cardamine hupingshanensis (SPCH). The purity, subunit composition, amino acid composition and matching
protein of SPCH were analyzed by using PAGE, SDS-PAGE, amino acid analyzer and matrix-assisted laser desorption/
ionization time of flight mass spectrometry (MALDI-TOF-MS). The anti-motor fatigue activity of SPCH was investigated by
measuring swimming time, blood lactic acid, hepatic glycogen and serum urea nitrogen in mice in weight-loaded swimming
test. Results showed that SPCH had three subunits with molecular weights of 37, 39 and 40 kD respectively. The matching
protein might be DING protein, predicted protein or chalcone synthase. The results also showed that SPCH significantly
prolonged the swimming time of mice (P < 0.01), decreased blood lactic acid content (P < 0.01), increased hepatic glycogen
content (P < 0.01), and reduced serum urea nitrogen content (P < 0.05). In conclusion, SPCH has a good anti-motor fatigue
activity as a dietary supplement.

Key words: Cardamine hupingshanensis, selenium-containing protein, purification, structure analysis, anti-motor fatigue activity