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

Authors: Chen Z-Y.; Zheng X-D.; Cao L.; Lu C-L.; Wu X-F.; He C.

Source: Protein and Peptide Letters, Volume 8, Number 2, April 2001 , pp. 131-138(8)

Publisher: Bentham Science Publishers

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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

Language: English

Document Type: Review article

DOI: http://dx.doi.org/10.2174/0929866013409553

Publication date: 2001-04-01

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Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.