Abstract
Studies of the interaction between Bikunin proteins, tumor necrosis factor-stimulated gene-6 protein (TSG-6), and glycosaminoglycans have revealed a unique catalytic activity where TSG-6/heavy chain 2 transfer heavy chain subunits between glycosaminoglycan chains. The activity is mediated by TSG-6/heavy chain 2 and involves a transient SDS stable interaction between TSG-6 and the heavy chain to be transferred. The focus of this study was to characterize the molecular structure of this cross-link to gain further insight into the catalytic mechanism. The result showed that the C-terminal Asp residue of the heavy chains forms an ester bond to Ser(28) beta-carbon of TSG-6 suggesting that this residue plays a role during catalysis.
Original language | English |
---|---|
Journal | Journal of Biological Chemistry |
Volume | 283 |
Issue | 49 |
Pages (from-to) | 33919-26 |
Number of pages | 8 |
ISSN | 0021-9258 |
DOIs | |
Publication status | Published - 5 Dec 2008 |
Keywords
- Carbon
- Catalysis
- Cell Adhesion Molecules
- Cell Line
- Cross-Linking Reagents
- Glycosaminoglycans
- Humans
- Mass Spectrometry
- Molecular Conformation
- Peptides
- Protein Binding
- Recombinant Proteins
- Serine
- Sodium Dodecyl Sulfate
- Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization