Decreased Heparin Sensitivity of Cyclohexanedione-Modified Thrombin
نویسندگان
چکیده
منابع مشابه
Heparin promotes the binding of thrombin to fibrin polymer. Quantitative characterization of a thrombin-fibrin polymer-heparin ternary complex.
The binding of human alpha-thrombin (IIa) to fibrin polymer (FnIIp) was studied in the presence and absence of a high affinity 20,300 Mr heparin (H) at pH 7.4, I 0.15, and 23 degrees C. In the absence of heparin, thrombin interacts with a high affinity class of binding sites on fibrin polymer with a dissociation constant of 301 +/- 36 nM in a manner which is independent of the enzyme active sit...
متن کاملKinetic analysis of the heparin-enhanced antithrombin III/thrombin reaction. Reaction rate enhancement by heparin-thrombin association.
The distribution of heparin between thrombin and antithrombin III in solutions containing both proteins has been calculated using a heparin-thrombin dissociation constant value, KgssMT, of 1.5 X lo-’ M and a heparin-antithrombin III dissociation constant value, KEgsMAT, of 2.0 x lo-’ M. The enhancing effect of heparin on the antithrombin III/thrombin reaction rate appeared to correlate with the...
متن کاملMolecular mapping of the heparin-binding exosite of thrombin.
Thrombin contains electropositive patches at opposite poles of the molecule which represent potential exosites for the binding of macromolecular ligands. The function of anion-binding exosite I, the fibrin(ogen) recognition site, has been well described. Anion-binding exosite II, located near the carboxyl terminus of the molecule, has been proposed to bind heparin on the basis of chemical modif...
متن کاملHeparin Promotes the Binding of Thrombin to Fibrin Polymer
The binding of human cr-thrombin (IIa) to fibrin polymer (FnIIp) was studied in the presence and absence of a high affinity 20,300 M, heparin (H) at pH 7.4,10.15, and 23 “C. In the absence of heparin, thrombin interacts with a high affinity class of binding sites on fibrin polymer with a dissociation constant of 301 f 36 nM in a manner which is independent of the enzyme active site. Studies of ...
متن کاملMolecular mapping of the thrombin-heparin cofactor II complex.
We used 55 Ala-scanned recombinant thrombin molecules to define residues important for inhibition by the serine protease inhibitor (serpin) heparin cofactor II (HCII) in the absence and presence of glycosaminoglycans. We verified the importance of numerous basic residues in anion-binding exosite-1 (exosite-1) and found 4 additional residues, Gln24, Lys65, His66, and Tyr71 (using the thrombin nu...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1978
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1978.tb12113.x