The Kinetics and Affinity of Binding of Glu-Plasminogen Specific to the ϵ-Amino Group ofl-Lysine: Its Potential Application to Modified Biomaterials
✍ Scribed by Peter H. Warkentin; Knut Johansen; John L. Brash; Ingemar Lundström
- Publisher
- Elsevier Science
- Year
- 1998
- Tongue
- English
- Weight
- 178 KB
- Volume
- 199
- Category
- Article
- ISSN
- 0021-9797
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✦ Synopsis
coagulation, plasmin should be generated at relatively high By covalently coupling L-lysine to an analytical surface through local concentrations, thus promoting the dissolution of incipa dipeptide linkage such that the e-amino group is accessible, we ient clots as they are formed. The material that we have have looked at plasminogen binding in real time. The results have developed for this purpose is based on a complex of dextran led to a model of plasminogen interactions with e-amino groups. with the dipeptide L-cysteinyl-L-lysine (CK-dextran). This
This paper focuses on the desorption kinetics of plasminogen ad-
choice is based on the knowledge that a key interaction in sorbed to this material. Plasminogen is shown to bind to the dipepthe fibrinolytic process is the interaction of plasminogen with tide in at least four different ways to the e-amino groups. It is the e-amino groups of lysine residues in fibrin (1).
suggested that some molecules bind to several e-amino groups at the same time. The surface plasmon resonance analysis also indi-Fibrinolysis, the removal of the fibrin clot, is accomcates that the interaction of Glu-plasminogen with L-lysine is very plished by the protein plasmin. The inactive proenzyme, complex and may not be defined simply by discrete kringle interacplasminogen, is cleaved to the active form plasmin by a tions alone. Dissociation constants ranging from 0.1 s 01 to less variety of activators, one of which is tissue-type plasminogen than 5 1 10 07 s 01 are observed. This material may well represent activator (tPA). Plasmin is then capable of dissolving the a surface sufficiently similar as to mimic plasminogen binding to blood clot to soluble fibrin degradation products (FDP). The fibrin.