Chem. J. Chinese Universities ›› 2003, Vol. 24 ›› Issue (8): 1472.

• Articles • Previous Articles     Next Articles

Spectroscopic Characterization of Glutathione S-Transferase of Asaphis dichotoma

YANG Hai-Ling, GAO Bo, ZENG Qing-Yin, FU Xue-Qi, NIE Li-Jia, ZHU Sheng-Geng, ZHOU Xian-Wan   

  1. 1. College of Life Sciences, Peking University, Beijing, 100871, China;
    2. College of Life Sciences, Jilin University, Changchun 130023, China
  • Received:2002-04-28 Online:2003-08-24 Published:2003-08-24

Abstract: AnoveLIsoenzyme of glutathione S-transferase(adGST) was purified from the liver intestine of the seashell(Asaphis dichotoma) by GST-Sepharose 4 Baffinity chromatography and reverse HPLC.The enzyme was composed of two subunits with a molecular weight of 23000 for each determined by SDS-PAGE, MALDITOF-MSand gel filtration.The characteristic peak of ultraviolet absorbance spectra of the ad GSTwas at 280 nm, and that of fluorescence excitation spectrum was at 280 nm and that of the fluorescence emission spectrum was at 350 nm.The CDspectra and FTIRspectroscopy show that the ad GSThas a total secondary structure content of about 35% α-helix and 30% sheets.The adGSTwas a kind of global protein.

Key words: Glutathione S-transferase(adGST), CD spectrum, FTIR spectrum, Secondary structure

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