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Human epidermal growth factor excreted by recombinant Escherichia coli K-12 has the correct N-terminus and is fully bioactive

Authors Huang, RC
Lam, E.
Chen, YH
Hackett, J. HKUST affiliated (currently or previously)
Lam, TL
Liu, D.
Ma, MC
Siu, KL
Sivakesava, S.
Xu, ZN
Wong, Raymond S C HKUST affiliated (currently or previously)
Wong, Wan Keung View this author's profile
Issue Date 1999
Source Process biochemistry , v. 35, (1-2), 1999, OCT, p. 1-5
Summary The high stability and productivity of recently-developed Escherichia coli JM101 strains expressing human epidermal growth factor (hEGF) facilitated scale-up of hEGF production, and a protocol to purify hEGF from bacterial culture supernatant was developed. hEGF-containing supernatant from an induced hEGF-expressing recombinant E. coli culture was purified by: (A) QAE Sephadex A-25 ion-exchange chromatography; (B) Sephadex G-25 desalting; (C) SP-Sepharose cation-exchange chromatography; and (D) reverse-phase HPLC. The hEGF obtained was pure by HPLC and SDS-PAGE. The N-terminus of the purified hEGF was authentic. Commercial pure hEGF, and hEGF purified as described, were assessed for bioactivity, and yielded superimposable curves. The recovery of hEGF with this protocol was 30\% of original, while the purity was 97-100\%. (C) 1999 Elsevier Science Ltd. All rights reserved.
ISSN 0032-9592
Rights Process Biochemistry © copyright (1999) Elsevier. The Journal's web site is located at
Language English
Format Article
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