NDLI: Cloning of HSA-GHGKHKNK fusion protein cDNA and its experssion in Pichia pastoris

Content Provider	IEEE Xplore Digital Library
Author	Yang Song Han Xiao An Liping Xu Guangyu Du Peige
Copyright Year	2011
Description	Author affiliation: Pharmaceutical College, Beihua University, Jilin, China (Yang Song; Han Xiao; An Liping; Xu Guangyu; Du Peige)
Abstract	GHGKHKNK octapeptide has tumoricidal potential mainly due to the amino acid residues of His-Gly-Lys motif inhibits the clone formation, adhesion and invasion of tumor cells. However, its clinical application is limited by its short half-life time in vivo. We used human serum albumin (HSA) fusion technology to fuse GHGKHKNK octapeptide and HSA to prolong half-life time of GHGKHKNK octapeptide and increase its stability. the GHGKHKNK — HSA fusion protein gene was cloned into the secretor type expression vector pPICZaC and subsequently expressed in Pichia pastoris. The supernatant fusion protein was detected by SDS-PAGE and purified with Blue Sepharose 6 Fast Flow chromatography. The clone formation rate of melanoma B16-F10 cell strain and the effect of the octapetide on the expression level of LN-R, ICAM-1 in melanoma B16-F10 cell strain were measured. Results suggested that infusion reaction between GHGKHKNK octapeptide and HSA did not destroy biologic activity of GHGKHKNK octapeptide.
Starting Page	1178
Ending Page	1181
File Size	286135
Page Count	4
File Format	PDF
ISBN	9781612847238
e-ISBN	9781612847269
DOI	10.1109/HHBE.2011.6029037
Language	English
Publisher	Institute of Electrical and Electronics Engineers, Inc. (IEEE)
Publisher Date	2011-08-19
Publisher Place	China
Access Restriction	Subscribed
Rights Holder	Institute of Electrical and Electronics Engineers, Inc. (IEEE)
Subject Keyword	Proteins Malignant tumors Humans Cloning Mice GHGKHKNK octapeptide Fusion protein Strain Half-life time
Content Type	Text
Resource Type	Article

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