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�й�ҩѧ��־ 2006, Vol. 41 Issue (13) :1029-1032    DOI:
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�㽭��ѧҩѧԺ������ҩ�о��� ���� 310031
WANG Guang-zhu��DING Ding��SUN Hong-ying��CHEN Shu-qing
Department of Biopharmaceutics��College of Pharmaceutical Sciences��Zhejiang University��Hangzhou 310031��China

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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.
Keywords�� Escherichia coli T-protein,   Chorismate mutase,   Prephenate dehydrogenase,   Polymerization status      
�ո�����: 2005-05-23;
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.�󳦸˾�T���׵ľۺ�״̬����[J]  �й�ҩѧ��־, 2006,V41(13): 1029-1032
.Polymerization Status Analysis of Escherichia coli T-protein [J]  Chinese Pharmaceutical Journal, 2006,V41(13): 1029-1032
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