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High-level expression and purification of active human FGF-2 in escherichia coli by codon and culture condition optimization
Joint Authors
Sulayman, Muhammad Rida
Khalili, Mustafa
Khansarinejad, Behzad
Baazm, Maryam
Source
Iranian Red Crescent Medical Journal
Issue
Vol. 18, Issue 2 (28 Feb. 2016), pp.1-8, 8 p.
Publisher
Publication Date
2016-02-28
Country of Publication
United Arab Emirates
No. of Pages
8
Main Subjects
Abstract EN
Basic fibroblast growth factor (bFGF) is a member of a highly conserved superfamily of proteins that are involved in cell proliferation, differentiation, and migration.
Objectives: The objective of this study was to overexpress and purify the high-level active human bFGF in Escherichia coli (E.
coli).
Materials and Methods: This experimental study was conducted in the Islamic Republic of Iran.
After codon optimization and gene synthesis, the optimized FGF-2 gene was subcloned into plasmid pET-32a.
pET32-FGF-2 was transformed into E.
coli BL21 for expression.
The cultivation parameters were optimized to produce a high yield of FGF-2.
Results: The optimal conditions were determined as follows: cultivation at 37°C in TB medium, with 1 mM isopropyl-β-D-thiogalactopyranoside (IPTG), followed by post-induction expression for 6 h.
Under the abovementioned conditions, the expression volumetric productivity of FGF-2 reached 1.48 g/L.
Conclusions: A fusion tag from the pET32 expression plasmid permits the recovery of the recombinant fusion FGF-2 from E.
coli, without affecting its biological activity.
American Psychological Association (APA)
Sulayman, Muhammad Rida& Khalili, Mustafa& Khansarinejad, Behzad& Baazm, Maryam. 2016. High-level expression and purification of active human FGF-2 in escherichia coli by codon and culture condition optimization. Iranian Red Crescent Medical Journal،Vol. 18, no. 2, pp.1-8.
https://search.emarefa.net/detail/BIM-654938
Modern Language Association (MLA)
Sulayman, Muhammad Rida…[et al.]. High-level expression and purification of active human FGF-2 in escherichia coli by codon and culture condition optimization. Iranian Red Crescent Medical Journal Vol. 18, no. 2 (Feb. 2016), pp.1-8.
https://search.emarefa.net/detail/BIM-654938
American Medical Association (AMA)
Sulayman, Muhammad Rida& Khalili, Mustafa& Khansarinejad, Behzad& Baazm, Maryam. High-level expression and purification of active human FGF-2 in escherichia coli by codon and culture condition optimization. Iranian Red Crescent Medical Journal. 2016. Vol. 18, no. 2, pp.1-8.
https://search.emarefa.net/detail/BIM-654938
Data Type
Journal Articles
Language
English
Notes
Includes bibliographical references : p. 7-8
Record ID
BIM-654938