A - Human Necessities – 61 – K
Patent
A - Human Necessities
61
K
A61K 38/48 (2006.01) A61K 38/16 (2006.01) A61K 38/36 (2006.01) A61K 38/55 (2006.01) A61K 39/395 (2006.01) C07K 14/75 (2006.01) C07K 14/81 (2006.01) C07K 16/36 (2006.01) C07K 16/40 (2006.01) C12N 9/74 (2006.01) A61K 38/00 (2006.01)
Patent
CA 2180140
Thrombus or clot formation and accretion are inhibited by administering thrombin-displacing substances to a patient. The thrombin- displacing substances comprise either thrombin analogs which bind to the thrombin-binding site on fibrin or fibrin analogs which bind to a fibrin-binding site on thrombin. By displacing the thrombin from clot or thrombus, the thrombin is released into circulation where it is inactivated by endogenous anti-proteinases. The fibrin analogs which bind to the fibrin-binding site on thrombin may be linked to a second binding moiety which binds to and/or inactivates the catalytic site and/or exosite I on thrombin to further inhibit thrombosis. The ability of test substances to displace thrombin is measured by exposure of the substance to immobilized thrombin-fibrin complex.
On inhibe la formation et l'accrétion de caillots ou de thrombus en administrant des substances de déplacement de thrombine à un patient. Ces substances comprennent soit des analogues de thrombine qui se lient à un site de liaison de thrombine sur la fibrine, soit des analogues de fibrine qui se lient à un site de liaison de fibrine sur la thrombine. Le déplacement de la thrombine hors du caillot ou du thrombus permet de libérer celle-ci dans la circulation sanguine, où elle est inactivée par des anti-protéinases endogènes. les analogues de fibrine qui se lient au site de liaison de fibrine sur la thrombine peuvent être rattachés à une seconde fraction de liaison qui se lie au site catalytique et/ou à un exosite I sur la thrombine et/ou qui inactive ce ou ces sites, afin d'assurer un inhibition accrue des thromboses. L'aptitude des substances d'essai à déplacer la thrombine est mesurée par exposition de la substance à un complexe thrombine-fibrine immobilisé.
Hirsh Jack
Weitz Jeffrey I.
Fetherstonhaugh & Co.
Hamilton Civic Hospitals Research Development Inc.
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