Tetranectin, a trimeric plasminogen‐binding C‐type lectin

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Abstract
Tetranectin, 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.