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KMID : 1094719970020020086
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Biotechnology and Bioprocess Engineering
1997 Volume.2 No. 2 p.86 ~ p.89
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Expression of recombinant epidermal growth factor inE. coli
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Yoon Chang-Shin
Lee Eun-Gyu
Lee Young-Seek
Chung Il-Yup
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Abstract
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Epidermal growth factor (EGF) known as a urgastrone is a powerful mitogen with a wide variety of possibilities for medical usages. A mature EGF coding region was isolated from human prepro-EGF sequence by a conventional PCR and cloned into pQE vector in which the gene product was supposed to be expressed with 6×His tag for the subsequent purification. The recombinant mature EGF was expressed in M15[Rep4], anEscherichia coli host strain, in amount of 30?40% of total proteins present inE. coli extract by the addition of isopropylthio-β-galactopyranoside (IPTG). The recombinant EGF purified using a Ni2+-NTA affinity column chromatography was active in its ability to induce phosphorylation on tyrosine residues of several substrate proteins when murine NIH3T3 and human MRC-5 fibroblast cells were stimulated with it. This work may provide the basic technology and information for the production of recombinant EGF.
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KEYWORD
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recombinant EGF, pQE, tyrosinephosphorylation
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