Polymerization Status Analysis of Escherichia coli T-protein
WANG Guang-zhu，DING Ding，SUN Hong-ying，CHEN Shu-qing
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Department of Biopharmaceutics，College of Pharmaceutical Sciences，Zhejiang University，Hangzhou 310031，China
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History+
Received
Published
2005-05-23
2006-07-05
Issue Date
2006-07-05
Abstract
OBJECTIVE To describe the tertiary structure of T-protein from Escherichia coli.METHODS T-protein,CM and PDH domains were cloned and expressed separately.The Mr determined by SDS-PAGE under denatured condition were 42×103,32×103 and 11×103 respectively for T-protein,PDH domain and CM domain,which were identical to the theoretical Mr.The calculated Mr of HPLC under the native condition were 63×103 and 25×103 respectively for PDH domain and CM domain.Chemical cross linking was employed to determine the polymerization status of T-protein,for its Mr was over-range in HPLC determination.RESULTS It is obvious that the Ms were doubled for PDH and CM domain under native condition.All of T-protein,CM and PDH are dimmers,Which was testified by both HPLC and chemical cross-linking experiments.CONCLUSION T-protein is a dimmer and it bonds together through adhesion of CM to CM and PDH to PDH domains.
WNG Gung-zhu;DING Ding;SUN Hong-ying;CHEN Shu-qing.
Polymerization Status Analysis of Escherichia coli T-protein [J]. Chinese Pharmaceutical Journal, 2006, 41(13): 1029-1032
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