| Autor: |
Holtet TL; Department of Molecular and Structural Biology, University of Aarhus, Denmark., Graversen JH, Clemmensen I, Thøgersen HC, Etzerodt M |
| Jazyk: |
angličtina |
| Zdroj: |
Protein science : a publication of the Protein Society [Protein Sci] 1997 Jul; Vol. 6 (7), pp. 1511-5. |
| DOI: |
10.1002/pro.5560060715 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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