Abstract:
:KGLP-1, a 31-amino acid glucagon-like peptide-1 (GLP-1) analogue, has a great therapeutic potential for anti-diabetes. In this work, a strategy for expression and purification of functional KGLP-1 peptide has been established. KGLP-1 cDNA was fused with glutathione S-transferase (GST), with an enterokinase cleavage site in the fusion junction. The recombinant fusion protein GST-KGLP-1 was affinity purified via the GST-tag, and then digested with enterokinase. The resulting GST part as well as the enzymes were eliminated by ultra-filtration followed by size exclusion chromatograph. The yield of purified KGLP-1 was approximately 12.1 mg/L, with purity of 96.18 %. The recombinant KGLP-1 was shown to have similar bioactivity as native GLP-1 when evaluated in a Chinese hamster ovary cell line expressing a GLP-1 receptor-egfp reporter gene.
journal_name
Biotechnol Lettjournal_title
Biotechnology lettersauthors
Liu Y,Ren L,Ge L,Cui Q,Cao X,Hou Y,Bai F,Bai Gdoi
10.1007/s10529-014-1526-1subject
Has Abstractpub_date
2014-08-01 00:00:00pages
1675-80issue
8eissn
0141-5492issn
1573-6776journal_volume
36pub_type
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