Journal ArticleDOI
The effect of fibrinogen degradation products and some lysine analogues on the dissociation of plasmin(ogen)-fibrin complexes.
S.A. Cederholm-Williams,A. Swain +1 more
TLDR
Fibrin carries sites which bind plasmin and preactivated plasmineogen allowing the formation of stable complexes suggesting that the plAsmin(ogen) binding site is present in this fragment of fibrinogen degradation product E.About:
This article is published in Thrombosis Research.The article was published on 1979-01-01. It has received 20 citations till now. The article focuses on the topics: Plasmin & Fibrinogen degradation product.read more
Citations
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Journal ArticleDOI
Activation of plasminogen by tissue activator is increased specifically in the presence of certain soluble fibrin(ogen) fragments.
TL;DR: The existence of a fibrin polymer is apparently not a prerequisite for this potentiating effect, and the plasminogen activation by various urokinase preparations is not potentiated by fibrIn and fibr in(ogen) fragments.
Journal ArticleDOI
Location of plasminogen-binding sites in human fibrin(ogen).
András Váradi,László Patthy +1 more
TL;DR: Competitive affinity chromatography of fragment D1 and fragments derived from it by proteolytic modification of its D gamma-chain revealed that this modification causes an 11-fold increase of the association constant of the interaction with Lys-plasminogen-Sepharose, which suggests that the carboxy-terminal region of the D Gamma-chain is involved in controlling the plasminagen-binding site of theD domain.
Journal ArticleDOI
Concentration of plasminogen and antiplasmin in plasma and serum
TL;DR: The concentrations of plasminogen and fast-acting antiplasmin were measured in 65 normal plasmas and matched sera and the decrease in plAsminogen level was due to both adsorption of pl asminogen to fibrin and reaction with antiplAsmin.
Journal ArticleDOI
Simple, rapid, and sensitive liquid chromatography-fluorescence method for the quantification of tranexamic acid in blood
José F. Huertas-Pérez,Michal Heger,Michal Heger,Henk L. Dekker,Hans Krabbe,Jan Lankelma,Freek Ariese +6 more
TL;DR: A high-performance liquid chromatography (HPLC)-fluorescence method was developed for the quantification of TA in blood and successfully applied to a heat-induced TA release study from thermosensitive liposomes.
Journal ArticleDOI
The binding of plasminogen to fibrin: Evidence for plasminogen-bridging
A.J. Garman,R.A.G. Smith +1 more
TL;DR: It is proposed that these effects are explicable in terms of a plasminogen-bridging model, in which the zymogen binds divalently between two monomer units of forming polymeric fibrin.
References
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Journal ArticleDOI
The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis
Klaus Weber,Mary Osborn +1 more
TL;DR: The results show that the polyacrylamide gel electrophoresis method can be used with great confidence to determine the molecular weights of polypeptide chains for a wide variety of proteins.
Journal ArticleDOI
Plasminogen: Purification from Human Plasma by Affinity Chromatography
Dale G. Deutsch,Edwin T. Mertz +1 more
TL;DR: Plasminogen was prepared from human plasma by affinity chromatography on L-lysine-substituted Sepharose with a specific activity of 100 caseinolytic units per milligram of nitrogen.
Journal ArticleDOI
Molecular mechanism of physiological fibrinolysis
TL;DR: A molecular model for the regulation of fibrinolysis in vivo is formulated and three hypotheses have been put forward to explain this specificity of plasmin, which has a greater affinity for fibrin than for its inhibitors.
Book ChapterDOI
Structural aspects of the fibrinogen to fibrin conversion.
TL;DR: This chapter focuses on the general shape of the native fibrinogen molecule and on the arrangement of the three pairs of nonidentical polypeptide chains that comprise the molecule and describes the relative locations of the amino and the carboxyterminals.
Journal ArticleDOI
Differences in the binding to fibrin of native plasminogen and plasminogen modified by proteolytic degradation influence of ω-aminocarboxylic acids
TL;DR: Evidence is provided that the decrease in binding of proteolytically degraded plasminogen may result in an inhibition of fibrinolysis caused by activators.
Related Papers (5)
Secondary-site binding of Glu-plasmin, Lys-plasmin and miniplasmin to fibrin
Elisabeth Suenson,Sixtus Thorsen +1 more
Sequence of formation of molecular forms of plasminogen and plasmin-inhibitor complexes in plasma activated by urokinase or tissue-type plasminogen activator.
Plasminogen: Purification from Human Plasma by Affinity Chromatography
Dale G. Deutsch,Edwin T. Mertz +1 more