Synthesis of an active hybrid growth factor (GF) in bacteria: transforming GF-alpha/vaccinia GF fusion protein
| Autor: | A. Greg Bruce, George J. Todaro, Lydia Wizental, A.F. Purchio, Daniel R. Twardzik, Shiu Lok Hu, Jane E. Ranchalis, Linda Madisen |
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| Rok vydání: | 1987 |
| Předmět: |
Peptide Biosynthesis
medicine.medical_treatment Recombinant Fusion Proteins Molecular Sequence Data DNA Recombinant Biology Gene product Epidermal growth factor Genetics medicine Escherichia coli Animals Amino Acid Sequence Peptide sequence DNA synthesis Base Sequence Growth factor Protein primary structure General Medicine Molecular biology Fusion protein Recombinant Proteins Biochemistry Transforming Growth Factors Intercellular Signaling Peptides and Proteins Peptides Cell Division Transforming growth factor |
| Zdroj: | Gene. 60(2-3) |
| ISSN: | 0378-1119 |
| Popis: | A hybrid gene encoding for a polypeptide consisting of the first 33 N-terminal amino acid (aa) residues of transforming growth factor-alpha (TGF-alpha) and a C terminus consisting of 20 aa residues of vaccinia growth factor (VGF) was chemically synthesized and expressed as a fusion protein in Escherichia coli. The primary structure of the hybrid gene product maintained the same positioning of the three disulfide bonds found in each parent molecule thus conserving the first two loop regions of TGF-alpha and the third loop region of VGF. After cleavage with CNBr its renatured biological activity was found to be comparable to TGF-alpha and VGF with respect to binding to the epidermal growth factor receptor, stimulation of DNA synthesis and induction of anchorage-independent growth of NRK cells in the presence of TGF-beta. Thus, we suggest that similar domains can be interchanged within the same family of molecules and equivalent functionality maintained. |
| Databáze: | OpenAIRE |
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