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https://hdl.handle.net/2440/11337
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Type: | Journal article |
Title: | Production and characterization of recombinant chicken insulin-like growth factor-II from E. coli |
Author: | Upton, Z. Kita, K. Wallace, J. Ballard, F. |
Citation: | Journal of Molecular Endocrinology, 1995; 14(1):79-90 |
Publisher: | Journal of Endocrinology Ltd. |
Issue Date: | 1995 |
ISSN: | 0952-5041 1479-6813 |
Abstract: | <jats:title>ABSTRACT</jats:title> <jats:p>Recombinant chicken (c)IGF-II has been produced in <jats:italic>Escherichia coli</jats:italic> after first modifying a plasmid that coded for a human (h)IGF-II fusion protein. The cIGF-II fusion protein, deposited in bacterial inclusion bodies, was dissolved under reducing conditions, desalted, subjected to anion-exchange chromatography and refolded. Recombinant cIGF-II was then released from the fusion protein using a genetically engineered serine protease and purified to homogeneity by reverse-phase HPLC. <jats:italic>In vitro</jats:italic> analysis of recombinant cIGF-II revealed differences between cIGF-II and its human counterpart. Recombinant cIGF-II was less potent than hIGF-II in stimulating protein synthesis in rat myoblasts. This appeared to be due to a decreased affinity for the type-1 IGF receptor. The human and chicken peptides were similar, however, in studies assessing binding to the type-2 IGF receptor and to IGF-binding proteins. Moreover, recombinant cIGF-II and hIGF-II were equipotent in both biological and receptor binding studies in chick embryo fibroblasts, suggesting that there may be a difference between mammalian and avian type-1 IGF receptors.</jats:p> |
DOI: | 10.1677/jme.0.0140079 |
Published version: | http://dx.doi.org/10.1677/jme.0.0140079 |
Appears in Collections: | Aurora harvest 7 Biochemistry publications |
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