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Heparin antithrombin

Like antithrombin, heparin cofactor II inhibits proteases by forming a I I stoichiometric complex with the enzyme. The protease attacks the reactive site of heparin cofactor II located on the C-terminus, resulting in the formation of a covalent bond. Heparin cofactor II has higher protease specificity than antithrombin. Of the coagulation enzymes, heparin cofactor II is known only to inhibit thrombin (92). Additionally heparin cofactor II has been shown to inhibit chymotrypsin (93) and leukocyte cathepsin G (94), This protease specificity appears to be due to the active site bond present in heparin cofactor II. Whereas antithrombin contains an Arg-Ser bond as its active site, heparin cofactor II is unique in containing a Leu-Ser bond. This suggests than another portion of the heparin cofactor II molecular may be required for protease binding,... [Pg.7]

Rosenberg RD, Damus PS. The purification and mechanism of action of human antithrombin-heparin cofactor. J Biol Chem 1973 248 6490-6505. [Pg.25]

Billett HH Direct and indirect antithrombins. Heparins, low molecular weight heparins, heparinoids,... [Pg.159]

Lahiri, B., Bagdasarian, A., Mitchell, B., Talamo, R. C., Colman, R. W. and Rosenberg, R. D, 1976, Antithrombin-Heparin Cofactor An inhibitor of plasma kallikrein. Archives of Biochemistry and Biophysics 175, 737- 747. [Pg.396]

FIGURE 7.13 (a) Modification of PUR surface with an antithrombin-heparin complex for blood contact, (b) influence of molecular weight of PEO used... [Pg.135]

K. Sask, L. Berry, A. Chan, J. Brash, Polyurethane modified with an antithrombin-heparin complex via polyethylene oxide linker/ spacers influence of PEO molecular weight and PEO-ATH bond on catalytic and direct anticoagulant functions, J. Biomed. Mater. Res. A 100 (10) (2012) 2821-2828. [Pg.143]

Highsmith, R.F., Rosenberg, R.D. The inhibition of human plasmin by human antithrombin-heparin cofactor. J. biol. Chem. 249, 4335-4338 (1974)... [Pg.422]

Du YJ, Brash JL, McClung G, Berry LR, Klement P, Chan AKC. Protein adsorption on polyurethane catheters modified with a novel antithrombin-heparin covalent complex. J Biomed Mater Res A 2007 80A 216-25. [Pg.70]

PEG-modifiedPU with antithrombin-heparin coating Multistep modification Different PEG intermediate layers ATH efficacy Static, in vitro Human plasma Good cell proliferation on ATH-PEG-OH-PU, antihrombin binding superior to fibrinogen [88]... [Pg.303]

The role of sialic acid residues in determining the life-time of circulating cells and glycoproteins and the importance of desialylation have been discussed, Chromatography on Blue Dextran 2000 coupled to agarose has been used in the rapid separation of factor X from citrated human plasma a 2(XX)-fold purification was achieved, Inhibition by the antithrombin-heparin cofactor of the conversion of factor IX into its active form by factor IXa has been examined. The process is time-dependent and requires a 1 1 combination... [Pg.317]

See other pages where Heparin antithrombin is mentioned: [Pg.119]    [Pg.254]    [Pg.79]    [Pg.194]    [Pg.254]    [Pg.33]    [Pg.119]    [Pg.134]    [Pg.270]    [Pg.349]    [Pg.303]    [Pg.296]    [Pg.301]    [Pg.303]   
See also in sourсe #XX -- [ Pg.47 , Pg.300 ]

See also in sourсe #XX -- [ Pg.47 , Pg.300 ]



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Antithrombin

Antithrombin III heparin cofactor

Antithrombin heparin binding

Antithrombin, heparin degradation

Antithrombin, interaction with heparin

Antithrombins

Heparin antithrombin 111 binding site

Heparin antithrombin-binding pentasaccharide

Heparin binding to antithrombin III

Heparin with antithrombin

Heparin-antithrombin complex

Heparin-protein interactions antithrombin

Synthesis of the Antithrombin-Binding Pentasaccharide Sequence in Heparin

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