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Bok, Robert Arnold 2014-12-15T23:43:48Z 2014-12-15T23:43:48Z 10000-01-01 1984 1984 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. http://hdl.handle.net/2142/70535 (UMI)AAI8502073 Chemistry, Biochemistry The Role of The Plasminogen-Fibrin Interaction in The Regulation of Fibrinolysis text Biochemistry Biochemistry University of Illinois at Urbana-Champaign Dissertation Ph.D.