CRCU

Chemical Research in Chinese Universities ›› 1995, Vol. 11 ›› Issue (2): 150-154.

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Studies on Increasing the Activity of Selenium-Containing Abzyme (Ⅰ)——Synthesis, Characterization and Properties of Hapten and Antigen

DING Lan1, ZHANG Guang-tian2, SUN Qi-an2, ZHU Zhen-qi2, LUO Gui-min2   

  1. 1. Laboratory of Rare Earth Chemistry and Physics, Changchun Instituteof Applied Chemistry, Academia Sinica, Changchun, 130024;
    2. The National Laboratory of Enzyme Engineering, Jilin University, Changchun, 130023
  • Received:1994-04-29 Online:1995-04-24 Published:2011-08-17

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Abstract: The thiol group of glutathione (GSH) reacts specifically with 2.4-di-m-trochlorobenzene to give S-substituted dinitrophenyl glutathione (GSH-S-DNP);two carboxyl groups of GSH-S-DNP were further esterified by n-butanol to produce the hapten,multisubstrate analog GSH-S-DNP Butyl Ester (GSH-S-DNP BE).The primary structure of the hapten was characterized by the free ammo group analysis,1H NMR,IRdeterminations and the elemental analysis.The hapten was then conjugated to bovine serum albumin (BSA) in the presence of glutaraldehyde.The reaction mixture was purified by Ultrogel AcA54 coluni chromatography to give the antigen.On an average,25 haptens were bound to each BSAmolecule.Electrophoresis analysis showed that the average molecular weight of the antigen was 87 KD.CDspectrum showed that the α-helix content of the antigen increased.

Key words: Glutathione peroxidase, Abzyme, Multisubstrate analog, Antigen, Hapten