Determination of the disulfide bond pairings in bovine transforming growth factor-α
| Autor: | Paul C. Toren, Bernard N. Violand, James F. Zobel, Christine E. Smith, Ned R. Siegel, Billy D. Vineyard, Jacob S. Tou, Paul D. Pyla, Eric W. Kolodziej |
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| Rok vydání: | 2009 |
| Předmět: |
chemistry.chemical_classification
Molecular Structure Protein Conformation Stereochemistry Molecular Sequence Data Thermolysin Transforming Growth Factor alpha Fast atom bombardment Mass spectrometry Biochemistry Mass Spectrometry Amino acid Dithiothreitol Protein structure chemistry Animals Molecule Organic chemistry Cattle Amino Acid Sequence Disulfides Protein disulfide-isomerase Peptide sequence Chromatography High Pressure Liquid |
| Zdroj: | International Journal of Peptide and Protein Research. 37:463-467 |
| ISSN: | 0367-8377 |
| DOI: | 10.1111/j.1399-3011.1991.tb00762.x |
| Popis: | A rapid method for determining the three disulfide bond pairings in bovine transforming growth factor-alpha (bTGF-alpha) was developed by digesting bTGF-alpha with thermolysin followed by separation of the generated peptides by reversed-phase HPLC. The disulfide-bonded peptides were identified by amino acid sequencing and fast atom bombardment mass spectrometry. The disulfide bond pairings in bTGF-alpha were determined to be homologous to those in the human and mouse TGF-alpha molecules. A species of low bioactivity isolated from the folding/oxidation mixture of chemically synthesized bTGF-alpha was demonstrated to contain two incorrect disulfide bonds. These results indicate that mispairing of disulfide bonds in bTGF-alpha significantly reduces the activity of this molecule. |
| Databáze: | OpenAIRE |
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