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Fusion Expression and Purification of OSBP PH Domain and Preliminary Analysis of Its Second Structure
1Department of Biochemstry and Molecular Biologhy, Fourth Military Medical University, Xi'an 710032, China. bioyao@Fmmu.edu.cn
Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao Acta Biochimica Et Biophysica Sinica
|May 30, 2002
Abstract:
Oxysterol binding protein (OSBP) is a regulator of oxysteroid metabolism. To investigate the function and the structure-function relationship of OSBP, the recombinant vector OSBP PH-pRSET-A was transformed into E.coli JM109(DE3), and the strain highly expressing soluble 6His-OSBP PH domain in minimal medium were obtained. The fusion protein was purified by Ni(2 )-NTA agarose beads. The secondary structure of the purified 6His-OSBP PH domain fusion protein was analysed by circular dichronism. The results indicated the PH domain was composed of alpha-helix 7.2%, beta-pleated sheets 71.1% and radom coil 21.7%.