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Determination of the disulfide bond pairings in bovine transforming growth factor-α

Content Provider	Scilit
Author	Violand, Bernard N. Tou, Jacob S. Vineyard, Billy D. Siegel, Ned R. Smith, Christine E. Pyla, Paul D. Zobel, James F. Toren, Paul C. Kolodziej, Eric W.
Copyright Year	2009
Description	Journal: International journal of peptide and protein research 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.
Related Links	http://onlinelibrary.wiley.com/doi/10.1111/j.1399-3011.1991.tb00762.x/pdf
Ending Page	467
Page Count	5
Starting Page	463
ISSN	03678377
DOI	10.1111/j.1399-3011.1991.tb00762.x
Journal	International journal of peptide and protein research
Issue Number	6
Volume Number	37
Language	English
Publisher	Wiley-Blackwell
Publisher Date	2009-01-12
Access Restriction	Open
Subject Keyword	Journal: International journal of peptide and protein research Bovine Transforming Growth Factor‐α Disulfide Bonds Mass Spectrometry Peptide Mapping
Content Type	Text
Resource Type	Article
Subject	Biochemistry

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