The characteristics of anticoagulation by covalently immobilized heparin.
The reactions of covalently immobilized heparin, abbreviated as I-Hep, with thrombin or Factor Xa were investigated both in the presence and absence of antithrombin III, AT III. Although I-Hep was able to bind to thrombin, the complex formation of thrombin and I-Hep did not affect the thrombin activity when measured by using a small artificial substrate, a peptide-MCA. Similarly, Factor Xa bound to I-Hep, but the activity of Factor Xa was not decreased in the absence of AT III, when a peptide-MCA was used for Factor Xa assay. Thrombin bound to I-Hep in much larger amounts than Factor Xa. Thrombin and Factor Xa were instantaneously inhibited by AT III in the presence of soluble heparin. However, when I-Hep was used instead of soluble heparin, instantaneous inhibition was not observed. When a natural, high-molecular-weight substrate was used for assay, the results were dependent on the structure of the immobilization carrier. Heparin immobilized on Sepharose 4B or Poly HEMA showed considerable prolongation of plasma recalcification time. However, heparin immobilized on the surface of PVA fiber did not prolong plasma recalcification time.
D000990:Antithrombin III / Q000494:pharmacology; D001672:Biocompatible Materials / Q000008:administration & dosage*; D001777:Blood Coagulation / Q000187:drug effects*; D005170:Factor X / Q000378:metabolism; D015951:Factor Xa; D006493:Heparin / Q000008:administration & dosage* / Q000494:pharmacology; D006801:Humans; D013917:Thrombin / Q000378:metabolism
D001672:Biocompatible Materials; D000990:Antithrombin III; D005170:Factor X; D006493:Heparin; D013917:Thrombin; D015951:Factor Xa