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Fibrinogen αC Domains Contain Cryptic Plasminogen and tPA Binding Sites
| Content Provider | Scilit |
|---|---|
| Author | Tsurupa, Galina Medved, Leonid |
| Copyright Year | 2006 |
| Description | Journal: Annals of the New York Academy of Sciences Surface plasmon resonance and ELISA experiments revealed that recombinant fibrinogen alpha C fragment (residues A alpha 221-610) corresponding to the alpha C domain binds tPA and plasminogen with high affinity. This binding was found to be Lys-dependent and occurred via independent binding sites. Study with truncated variants of the alpha C fragment located these sites in its COOH-terminal half. Binding of tPA and plasminogen to these sites stimulated activation of the latter whereas proteolytic degradation of the alpha C fragment reduced this effect substantially, suggesting the importance of the alpha C domains in regulation of fibrinolysis. |
| Related Links | http://onlinelibrary.wiley.com/doi/10.1111/j.1749-6632.2001.tb03518.x/pdf |
| Ending Page | 330 |
| Page Count | 3 |
| Starting Page | 328 |
| e-ISSN | 17496632 |
| DOI | 10.1111/j.1749-6632.2001.tb03518.x |
| Journal | Annals of the New York Academy of Sciences |
| Issue Number | 1 |
| Volume Number | 936 |
| Language | English |
| Publisher | Wiley-Blackwell |
| Publisher Date | 2006-01-25 |
| Access Restriction | Open |
| Subject Keyword | Journal: Annals of the New York Academy of Sciences Biochemistry and Molecular Biology |
| Content Type | Text |
| Resource Type | Article |