Use this URL to cite or link to this record in EThOS: https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.751036
Title: The high affinity calcium binding sites in fibrinogen
Author: Ross, Joan
Awarding Body: University of St Andrews
Current Institution: University of St Andrews
Date of Award: 1983
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Abstract:
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.
Supervisor: Kemp, Graham Sponsor: Biotechnology and Biological Sciences Research Council (BBSRC)
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID: uk.bl.ethos.751036  DOI: Not available
Keywords: QP93.5R7 ; Blood--Coagulation
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