About: High-level expression and purification of soluble recombinant FGF21 protein by SUMO fusion in Escherichia coli

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About: High-level expression and purification of soluble recombinant FGF21 protein by SUMO fusion in Escherichia coli Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	High-level expression and purification of soluble recombinant FGF21 protein by SUMO fusion in Escherichia coli
Creator	Li, Xiaokun Huang, Yadong Zhao, Hongxin Fu, Lianjun Gao, Hongchang Qin, Yuxia Wan, Xiaoshan Wang, Huiyan Xiao, Yechen Zhang, Yaofang
Source	Medline; PMC
abstract	BACKGROUND: Fibroblast growth factor 21 (FGF21) is a promising drug candidate to combat metabolic diseases. However, high-level expression and purification of recombinant FGF21 (rFGF21) in Escherichia coli (E. coli) is difficult because rFGF21 forms inclusion bodies in the bacteria making it difficult to purify and obtain high concentrations of bioactive rFGF21. To overcome this problem, we fused the FGF21 with SUMO (Small ubiquitin-related modifier) by polymerase chain reaction (PCR), and expressed the fused gene in E. coli BL21(DE3). RESULTS: By inducing with IPTG, SUMO-FGF21 was expressed at a high level. Its concentration reached 30% of total protein, and exceeded 95% of all soluble proteins. The fused protein was purified by DEAE sepharose FF and Ni-NTA affinity chromatography. Once cleaved by the SUMO protease, the purity of rFGF21 by high performance liquid chromatography (HPLC) was shown to be higher than 96% with low endotoxin level (<1.0 EU/ml). The results of in vivo animal experiments showed that rFGF21 produced by using this method, could decrease the concentration of plasma glucose in diabetic rats by streptozotocin (STZ) injection. CONCLUSIONS: This study demonstrated that SUMO, when fused with FGF21, was able to promote its soluble expression of the latter in E. coli, making it more convenient to purify rFGF21 than previously. This may be a better method to produce rFGF21 for pharmaceutical research and development.
has issue date	2010-02-17(xsd:dateTime)
bibo:doi	10.1186/1472-6750-10-14
bibo:pmid	20163718
has license	cc-by
sha1sum (hex)	b187316c24eb26f96af6ebbc243e90cfc504d94b
schema:url	https://doi.org/10.1186/1472-6750-10-14
resource representing a document's title	High-level expression and purification of soluble recombinant FGF21 protein by SUMO fusion in Escherichia coli
has PubMed Central identifier	PMC2831817
has PubMed identifier	20163718
schema:publication	BMC Biotechnol
resource representing a document's body	covid:b187316c24eb26f96af6ebbc243e90cfc504d94b#body_text
is schema:about of	named entity 'PROTEIN ' named entity 'HIGH' named entity 'RECOMBINANT' named entity 'HIGH LEVEL' named entity 'BACKGROUND' named entity 'SOLUBLE' named entity 'BL21' named entity 'RATS' named entity 'NTA' named entity 'POLYMERASE CHAIN REACTION' named entity 'ANIMAL EXPERIMENTS' named entity 'IPTG' named entity 'NI-' named entity 'LIQUID CHROMATOGRAPHY ' named entity 'IS A' named entity 'DEAE' named entity 'PURITY' named entity 'PROBLEM' named entity 'ENDOTOXIN' named entity 'FGF21' named entity 'SUMO' named entity 'METABOLIC DISEASES' named entity 'LOW' named entity 'E. COLI' named entity 'PLASMA GLUCOSE' named entity 'DIFFICULT' named entity 'OVERCOME' named entity '30%' named entity 'INDUCING' named entity 'PURIFICATION' named entity 'CANDIDATE' named entity 'OBTAIN' named entity 'USING' named entity 'HIGH' named entity 'LEVEL' named entity 'ITS' named entity 'DRUG' named entity 'COMBAT' covid:arg/b187316c24eb26f96af6ebbc243e90cfc504d94b named entity 'EXPRESSION' named entity 'FGF21' named entity 'LEVEL' named entity 'FUSION' named entity 'SUMO' named entity 'PURIFICATION' named entity 'ESCHERICHIA COLI' named entity 'PROTEIN ' named entity 'UBIQUITIN-RELATED' named entity 'HIGH PERFORMANCE LIQUID CHROMATOGRAPHY' named entity 'RESULTS' named entity 'STREPTOZOTOCIN' named entity 'EXPRESSED' named entity 'METHOD' named entity 'SEPHAROSE' named entity 'FUSED' named entity 'CONCENTRATION OF' named entity 'CLEAVED' named entity 'CONCENTRATIONS' named entity 'PURIFIED' named entity 'FORMS' named entity 'PROTEINS' named entity 'CONCENTRATION' named entity 'BACTERIA ' named entity 'FIBROBLAST GROWTH FACTOR 21' named entity 'MODIFIER' named entity 'EXPRESSION' named entity 'TOTAL PROTEIN' named entity 'DIABETIC' named entity 'RECOMBINANT' named entity 'ESCHERICHIA COLI' named entity 'SOLUBLE' named entity 'IN VIVO'

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