NATURAL PRODUCT RESEARCH AND DEVELOPMENT ›› 2012, Vol. 23 ›› Issue (8): 1020-. doi: A

• Article • Previous Articles     Next Articles

Purification and Identification of a Novel Protein with Antitumor Activity from Peganum harmala Seeds

MA Xiao-jin, WU Ting, LUO Jing-jing, WANG Yang, LI Yang, LIU Dong-liang, SUN Su-rong*   

  1. Xinjiang Key Laboratory of Biological Resources and Genetic Engineering, College of Life Science and Technology, Xinjiang University, Urumqi 830046, China
  • Online:2012-09-06 Published:2012-10-15

Abstract: A novel protein with anti-proliferative activity, namaly PhLTP, was isolated from Peganum harmala seeds by a combined procedure involving extraction, ammonium sulfate precipitation, ion exchange chromatography on CM-Sepharose and gel-filtration on Superdex 75. The apparent molecular mass of the purified Peganum harmala protein was 14.8 kDa, with comprising of homodimer. It has similar N-terminal amino acid sequences with non-specific lipid transfer proteins (nsLTPs) of the other plants using NCBI Blast searching for short. PhLTP showed anti-proliferative activity towards some well established cancer cell lines, e.g. Eca-109, MGC-9, BEL-740, and HeLa. The inhibitory effect on the HeLa cell viability was dependent on both concentration and time, and the hemi-inhibitory concentration was 45μg/mL after 48 hour. PhLTP was also found that this protein induced apoptosis in HeLa cells as evidenced by cell morphological analysis.

Key words: Peganum harmala, lipid transfer proteins, purification, antitumor, apoptosis

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