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作 者:SONG Hao-wei XU Chong-feng FU Yun-lin YANG Peng-yuan WANG Hong-hai
机构地区:[1]Department of Chemistry [2]State Key Laboratory of Genetic Engineering,Fudan University,Shanghai 200433,P.R.China
出 处:《Chemical Research in Chinese Universities》2001年第4期387-393,共7页高等学校化学研究(英文版)
基 金:NFS of China(No.29927002)and Visiting Scholar Foundation of Key Lab. in University.
摘 要: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.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.
关 键 词:UNFOLDING LYSOZYME Reduction and alkylation Time-resolved ESI-MS
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