title: [Binding of lys-plasminogen to E-fragment of fibrinogen].
abstract: The interaction of Lys-plasminogen and its fragments with fibrinogen fragment E was studied by equilibrium affinity binding. A quantitative analysis of binding parameters revealed two types of binding sites responsible for Lys-plasminogen interaction with the immobilized fragment E, i.e., with a high (Kd = 1.5 x 10(-6) M) and low (Kd = 82 x 10(-6) M) affinity ones. Among plasminogen fragments, only miniplasminogen and KI-3 bound immobilized fragment E and were eluted by epsilon-aminocaproic acid. Hence, two lysine binding sites may be involved in the binding of Lys-plasminogen to fragment E; they are localized in the KI-3 and K5 kringle structures.
authors.forename: S A
authors.initials: SA
authors.lastname: Kudinov
authors.forename: S I
authors.initials: SI
authors.lastname: Andrianov
authors.forename: T I
authors.initials: TI
authors.lastname: Lezhen
mesh_terms: D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D005338:Fibrin Fibrinogen Degradation Products / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D010446:Peptide Fragments / Q000378:metabolism*; D010958:Plasminogen / Q000378:metabolism*
chemical_list: D005338:Fibrin Fibrinogen Degradation Products; D010446:Peptide Fragments; C018543:fibrinogen fragment E; C018998:lysyl-plasminogen; D010958:Plasminogen
vernacular_title: Sviazyvanie liz-plazminogena s E-fragmentom fibrinogena.