Tetranectin, a plasminogen-binding protein belonging to the family of
C-type lectins, was expressed in E. coli and converted to its native f
orm by in vitro refolding and proteolytic processing. Recombinant tetr
anectin-as well as natural tetranectin from human plasma-was shown by
chemical cross-linking analysis and SDS-PAGE to be a homo-trimer in so
lution as are other known members of the collectin family of C-type le
ctins. Biochemical evidence is presented showing that an N-terminal do
main encoded within exons 1 and 2 of the tetranectin gene is necessary
and sufficient to govern subunit trimerization.