{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/70535"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/70535","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"The Role of The Plasminogen-Fibrin Interaction in The Regulation of Fibrinolysis","abstract":"Fibrinolysis refers to the proteolytic mechanism whereby the body dissoloves intravascular deposits of fibrin, a process important in maintaining the patency of the circulatory system. The major components of the fibrinolytic system, plasminogen and plasminogen activator, are known to co-exist in the blood but the biochemical details of how the proteolytic system is regulated to restrict plasmin formation to the sites of fibrin clots are not well understood. A possible mechanism of regulation involves the complexation of plasminogen with fibrin. To investigate the relevance of such a mechanism, the binding of Glu-plasminogen and Lys-plasminogen to fibrin, to immobilized lysine and to plasmin-cleaved fibrin were quantitatively characterized. The effects of two forms of fibrin on the activation kinetics of Glu- and Lys-plasminogen were also studied. The binding studies were performed using radioisotopically labelled plasminogen. A synthetic, fluorogenic substrate for plasmin was employed in the kinetic studies. Both forms of plasminogen displayed a physiologically relevant affinity for fibrin and limited plasmic cleavage of fibrin created new binding sites for plasminogen. This plasmin-created site is probably indentical to the functional moiety found on lysine-Sepharose. Fibrin possessed the capacity to significantly stimulate Glu-plasminogen activation by urokinase. A large decrease in the Michaelis constant (K(,m)) for activation occurred in the presence of fibrin, which in the lower, physiological range of Glu-plasminogen concentrations resulted in an enhanced rate of activation.","abstract_html":"Fibrinolysis refers to the proteolytic mechanism whereby the body dissoloves intravascular deposits of fibrin, a process important in maintaining the patency of the circulatory system. The major components of the fibrinolytic system, plasminogen and plasminogen activator, are known to co-exist in the blood but the biochemical details of how the proteolytic system is regulated to restrict plasmin formation to the sites of fibrin clots are not well understood. A possible mechanism of regulation involves the complexation of plasminogen with fibrin. To investigate the relevance of such a mechanism, the binding of Glu-plasminogen and Lys-plasminogen to fibrin, to immobilized lysine and to plasmin-cleaved fibrin were quantitatively characterized. The effects of two forms of fibrin on the activation kinetics of Glu- and Lys-plasminogen were also studied. The binding studies were performed using radioisotopically labelled plasminogen. A synthetic, fluorogenic substrate for plasmin was employed in the kinetic studies. Both forms of plasminogen displayed a physiologically relevant affinity for fibrin and limited plasmic cleavage of fibrin created new binding sites for plasminogen. This plasmin-created site is probably indentical to the functional moiety found on lysine-Sepharose. Fibrin possessed the capacity to significantly stimulate Glu-plasminogen activation by urokinase. A large decrease in the Michaelis constant (K(,m)) for activation occurred in the presence of fibrin, which in the lower, physiological range of Glu-plasminogen concentrations resulted in an enhanced rate of activation.","abstract_has_math":false,"creators":["Bok, Robert Arnold"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Biochemistry","degree_department":null,"school":null,"contributors":[],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2014,"date_issued":"2014-12-15T23:43:48Z","date_published":"2014-12-15T23:43:48Z","updated_at":"2026-07-22T22:26:03Z","subjects":["Chemistry, Biochemistry"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(UMI)AAI8502073"],"render_values":[{"text":"(UMI)AAI8502073","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/70535","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:creator","label":"Author","values":["Bok, Robert Arnold"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2014-12-15T23:43:48Z","10000-01-01","1984"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biochemistry"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Dissertation"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Ph.D."]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["University of Illinois at Urbana-Champaign"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Chemistry, Biochemistry"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["http://hdl.handle.net/2142/70535","(UMI)AAI8502073"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Fibrinolysis refers to the proteolytic mechanism whereby the body dissoloves intravascular deposits of fibrin, a process important in maintaining the patency of the circulatory system. The major components of the fibrinolytic system, plasminogen and plasminogen activator, are known to co-exist in the blood but the biochemical details of how the proteolytic system is regulated to restrict plasmin formation to the sites of fibrin clots are not well understood. A possible mechanism of regulation involves the complexation of plasminogen with fibrin. To investigate the relevance of such a mechanism, the binding of Glu-plasminogen and Lys-plasminogen to fibrin, to immobilized lysine and to plasmin-cleaved fibrin were quantitatively characterized. The effects of two forms of fibrin on the activation kinetics of Glu- and Lys-plasminogen were also studied. The binding studies were performed using radioisotopically labelled plasminogen. A synthetic, fluorogenic substrate for plasmin was employed in the kinetic studies. Both forms of plasminogen displayed a physiologically relevant affinity for fibrin and limited plasmic cleavage of fibrin created new binding sites for plasminogen. This plasmin-created site is probably indentical to the functional moiety found on lysine-Sepharose. Fibrin possessed the capacity to significantly stimulate Glu-plasminogen activation by urokinase. A large decrease in the Michaelis constant (K(,m)) for activation occurred in the presence of fibrin, which in the lower, physiological range of Glu-plasminogen concentrations resulted in an enhanced rate of activation.","Made available in DSpace on 2014-12-15T23:43:48Z (GMT). No. of bitstreams: 1 8502073.pdf: 4412935 bytes, checksum: 217133f8159b143343bb2bc51a842c22 (MD5) Previous issue date: 1984","Embargo set by: Seth Robbins for item 70701 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs","Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs","U of I Only","150 p.","Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1984."]},{"key":"dc:title","label":"Title","values":["The Role of The Plasminogen-Fibrin Interaction in The Regulation of Fibrinolysis"]}]}],"canonical_facts":{"dc:creator":["Bok, Robert Arnold"],"dc:date":["2014-12-15T23:43:48Z","10000-01-01","1984"],"dc:description":["Fibrinolysis refers to the proteolytic mechanism whereby the body dissoloves intravascular deposits of fibrin, a process important in maintaining the patency of the circulatory system. The major components of the fibrinolytic system, plasminogen and plasminogen activator, are known to co-exist in the blood but the biochemical details of how the proteolytic system is regulated to restrict plasmin formation to the sites of fibrin clots are not well understood. A possible mechanism of regulation involves the complexation of plasminogen with fibrin. To investigate the relevance of such a mechanism, the binding of Glu-plasminogen and Lys-plasminogen to fibrin, to immobilized lysine and to plasmin-cleaved fibrin were quantitatively characterized. The effects of two forms of fibrin on the activation kinetics of Glu- and Lys-plasminogen were also studied. The binding studies were performed using radioisotopically labelled plasminogen. A synthetic, fluorogenic substrate for plasmin was employed in the kinetic studies. Both forms of plasminogen displayed a physiologically relevant affinity for fibrin and limited plasmic cleavage of fibrin created new binding sites for plasminogen. This plasmin-created site is probably indentical to the functional moiety found on lysine-Sepharose. Fibrin possessed the capacity to significantly stimulate Glu-plasminogen activation by urokinase. A large decrease in the Michaelis constant (K(,m)) for activation occurred in the presence of fibrin, which in the lower, physiological range of Glu-plasminogen concentrations resulted in an enhanced rate of activation.","Made available in DSpace on 2014-12-15T23:43:48Z (GMT). No. of bitstreams: 1 8502073.pdf: 4412935 bytes, checksum: 217133f8159b143343bb2bc51a842c22 (MD5) Previous issue date: 1984","Embargo set by: Seth Robbins for item 70701 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs","Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs","U of I Only","150 p.","Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1984."],"dc:identifier":["http://hdl.handle.net/2142/70535","(UMI)AAI8502073"],"dc:subject":["Chemistry, Biochemistry"],"dc:title":["The Role of The Plasminogen-Fibrin Interaction in The Regulation of Fibrinolysis"],"dc:type":["text"],"thesis:degree_discipline":["Biochemistry"],"thesis:degree_level":["Dissertation"],"thesis:degree_name":["Ph.D."],"thesis:institution_name":["University of Illinois at Urbana-Champaign"]},"updated_at":"2026-07-22T22:26:03Z"}