A purification method to obtain a fibrinogen preparation with a high proportion of intact molecules and free from contaminating plasminogen and Factor XIII was developed. Such fibrinogen preparations were used in cross-linking and plasmin-digestion studies to investigate the possible involvement of the carboxyl terminal regions of the A-chain in a high affinity calcium-binding site. The results of these investigations gave no evidence to support such a role for the carboxyl terminals of the A-chains. Highly intact fibrinogen preparations were also used in experiments to re-assess the number of high affinity calcium-binding sites in the molecule. The technique of flow dialysis was employed. Results from these experiments were in agreement with previously published data that there are three high affinity calcium-binding sites in fibrinogen. Indirect evidence was obtained which suggests that the chelator EGTA binds to the fibrinogen molecule.
| Identifer | oai:union.ndltd.org:bl.uk/oai:ethos.bl.uk:751036 |
| Date | January 1983 |
| Creators | Ross, Joan |
| Contributors | Kemp, Graham |
| Publisher | University of St Andrews |
| Source Sets | Ethos UK |
| Detected Language | English |
| Type | Electronic Thesis or Dissertation |
| Source | http://hdl.handle.net/10023/14913 |
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