Chemical synthesis of bovine transforming growth factor-α: Synthesis, characterization and biological activity
Autor: | Larry A. Kaempfe, M.F. McGrath, John C. Byatt, Billy D. Vineyard, Jacob S. Tou, Bernie N. Violand, Mark E. Zupec |
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Rok vydání: | 1990 |
Předmět: |
Protein Conformation
medicine.medical_treatment Molecular Sequence Data Biophysics Peptide Peptide Mapping Biochemistry Chemical synthesis Epithelium Mass Spectrometry Mammary Glands Animal Species Specificity Sequence Homology Nucleic Acid medicine Animals Humans Amino Acid Sequence Molecular Biology Peptide sequence Chromatography High Pressure Liquid chemistry.chemical_classification Chemistry Cell growth Growth factor Epithelial Cells Biological activity Cell Biology Rats Amino acid ErbB Receptors Kinetics Liver Transforming Growth Factors Cattle Indicators and Reagents Cell Division Transforming growth factor |
Zdroj: | Biochemical and Biophysical Research Communications. 167:484-491 |
ISSN: | 0006-291X |
DOI: | 10.1016/0006-291x(90)92049-6 |
Popis: | Bovine transforming growth factor-alpha (bTGF-alpha) is a 50 amino acid polypeptide with three disulfide linkages. In order to evaluate the biological function of this peptide, bTGF-alpha was synthesized via an automatic synthesizer and purified to homogeneity in high yield. The integrity of this synthetic peptide was confirmed by chemical analyses and bioassays. In a bovine liver radioreceptor assay, bTGF-alpha competes with radiolabeled EGF and has activity comparable to mEGF and hTGF-alpha. Compared to hEGF, bTGF-alpha elicits a greater response in a bovine mammary cell proliferation. |
Databáze: | OpenAIRE |
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