Chem. J. Chinese Universities

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Purification and Properties of Recombinant Ganoderma Lucidum Immunoregulatory Protein

ZHU Jian-Qiang2, LIANG Chong-Yang1, FENG Kai2, GAI Xiao-Dong2, SUN Xin2, SUN Fei1*   

    1. Institute of Regenerative Medical Science, School of Pharmaceutical Sciences, Jilin University, Changchun 130021, China;
    2. Center of Life Science, Beihua University, Jilin 132013, China
  • Received:2007-07-09 Revised:1900-01-01 Online:2008-04-10 Published:2008-04-10
  • Contact: SUN Fei

Abstract: Recombinant Ganoderma lucidum immunoregulatory protein(rGlip) was purified from fermentation. Purification was carried out by ultrafiltration, anion exchange chromatography(AIEC), hydrophobic interaction chromatography(HIC), size exclusion chromatography(SEC). We used Hitrap Q sepharose column to measure the optimal pH value of anion exchange chromatography and detect the absorption value of protein at 215, 254, 280 nm. The intensity absorption of rGlip was found at 215 nm. Hemagglutination reactionno aggregation was observed between any types of human red blood cells, the positive activity was seen in the presence of sheep blood red cells. The optimal pH of AIEC enhanced the yield of initial purification, HIC was designed for lyophobic domains of rGlip, and end product(rGlip) of purification procedures possessed aggregation activity of sheep red blood cells.

Key words: Ganoderma lucidum, Anion exchange chromatography, Hydrophobic interaction chromatography, Size exclusion chromatography, Purification

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