Production, Purification, and Biological Activity Analysis of Recombinant Human Persephin Expressed in Insect Cells

Author(s): Zhe-Yu Chen, Xing-Dong Zheng, Li Cao, Chang-Lin Lu, Xiang-Fu Wu, Cheng He.

Journal Name: Protein & Peptide Letters

Volume 8 , Issue 2 , 2001

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Abstract:

Recombinant human Persephin (PSP) has been expressed at high levels in recombinant baculavirus infected Trichoplusia ni (Tn-5B1-4) cells. The expressed protein was purified by nickel affinity chromatography. Pure, recombinant human PSP promoted the survival of embryonic motor neurons in vitro but failed to protect adult rat spinal cord motor neurons after sciatic nerve transection in vivo. Because recombinant bioactive human PSP can be obtained in large quantities, and purified to near homogeneity, they are suitable for further biological activity investigation.

Keywords: human persephin, human persephin psp, trichoplusia ni, neurturin NTN

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Article Details

VOLUME: 8
ISSUE: 2
Year: 2001
Page: [131 - 138]
Pages: 8
DOI: 10.2174/0929866013409553
Price: $58

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