Chem. J. Chinese Universities ›› 2002, Vol. 23 ›› Issue (5): 818.

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Studies on a New Method of Extraction and Purification of Troponin Ⅰ

MA Xue-Hua, LIU Zhong-Ying, HU Xiu-Li, SHI Yi, JIANG Xi-Luo, AN Ru-Guo   

  1. Institute of Biological Engineering, Jilin University, Changchun 130021, China
  • Received:2001-01-08 Online:2002-05-24 Published:2002-05-24

Abstract: Rabbit skeletal muscle was homogenized and centrifuged, then applied to DEAE-Sephadex A25, Sephadex G75 and Butyl Sepharose columns in turn.Finally, the purified sTnCwas obtained.The affinity chromatography gel was prepared by binding the purified sTnConto the CNBr-act Sepharose 4B.Troponin Iwas isolated directly from whole skeletal and cardial muscle by using the affinity chromatography gel.Both the results of HPLCand SDS-PAGEshow a single band.The molecular weights of the purified sTn Iand cTn Iwere 21000 and 25000, respectively.The yield of sTnCwas 82.6 mg/100 g cardiac tissue, which was higher than that obtained by using the previous method.In this work, 91.6 mg purified cTn Iwere obtained.

Key words: sTnC, sTn I, cTn I, Purification

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