Tetranectin, a trimeric plasminogen‐binding C‐type lectin
Copyright policy )Tetranectin, a trimeric plasminogen‐binding C‐type lectin
AbstractTetranectin, a plasminogen‐binding protein belonging to the family of C‐type lectins, was expressed in E. coli and converted to its native form by in vitro refolding and proteolytic processing. Recombinant tetranectin—as well as natural tetranectin from human plasma—was shown by chemical cross‐linking analysis and SDS‐PAGE to be a homo‐trimer in solution as are other known members of the collectin family of C‐type lectins. Biochemical evidence is presented showing that an N‐terminal domain encoded within exons 1 and 2 of the tetranectin gene is necessary and sufficient to govern subunit trimerization.
- Aarhus University Denmark
- Rigshospitalet Denmark
- Statens Serum Institut Denmark
Protein Folding, Sequence Homology, Amino Acid, Protein Conformation, Placenta, Recombinant Fusion Proteins, Molecular Sequence Data, Plasminogen, Blood Proteins, Sequence Analysis, DNA, Solutions, Cross-Linking Reagents, Pregnancy, Lectins, Escherichia coli, Humans, Female, Lectins, C-Type, Amino Acid Sequence, Cloning, Molecular, Protein Processing, Post-Translational
Protein Folding, Sequence Homology, Amino Acid, Protein Conformation, Placenta, Recombinant Fusion Proteins, Molecular Sequence Data, Plasminogen, Blood Proteins, Sequence Analysis, DNA, Solutions, Cross-Linking Reagents, Pregnancy, Lectins, Escherichia coli, Humans, Female, Lectins, C-Type, Amino Acid Sequence, Cloning, Molecular, Protein Processing, Post-Translational
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