| Literature DB >> 9232652 |
T L Holtet1, J H Graversen, I Clemmensen, H C Thøgersen, M Etzerodt.
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.Entities:
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Year: 1997 PMID: 9232652 PMCID: PMC2143742 DOI: 10.1002/pro.5560060715
Source DB: PubMed Journal: Protein Sci ISSN: 0961-8368 Impact factor: 6.725