CRCU

Chemical Research in Chinese Universities ›› 2001, Vol. 17 ›› Issue (4): 387-393.

• Articles • Previous Articles     Next Articles

Time-resolved ESI-MS Investigation on Reduction and Alkylation in Unfolding Process of Lysozyme

SONG Hao-wei1,2, XU Chong-feng1, FU Yun-lin1, YANG Peng-yuan1,2, WANG Hong-hai2   

  1. 1. Department of Chemistry Fudan University, Shanghai 200433, P. R. China;
    2. State Key Laboratory of Genetic Engineering, Fudan University, Shanghai 200433, P. R. China
  • Received:2001-09-21 Online:2001-12-24 Published:2011-08-04
  • Supported by:

    Supported by the NFS of China(No.29927002) and Visiting Scholar Foundation of Key Lab. in University.

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Abstract: The kinetic procedure of the unfolding of lysozyme induced by the reduction of disulfide was monitored by the time-resolved ESI-MS with a sheath liquid assistant electrospray interface.It was found that the reduction process for the eight disulfides had a less difference in the reaction time after denatured treatment.In addition, the alkylation of the reduced free thiols was much slower than the reduction procedure.An artifact peak produced by the CID fragmentation in the mass spectra was identified and the possible mechanism of the Hofmann elimination reaction was proposed.

Key words: Unfolding, Lysozyme, Reduction and alkylation, Time-resolved ESI-MS