Results 201 to 210 of about 37,722 (251)
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Molecular Medicine Today, 1995
Antithrombin, the main inhibitor of thrombosis in blood, is bound and activated by the heparin-like side-chains that line the small vasculature. We now have good depictions of the heparin-binding site on antithrombin, and of the way in which mutations at this site cause thrombotic disease.
R, Carrell +3 more
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Antithrombin, the main inhibitor of thrombosis in blood, is bound and activated by the heparin-like side-chains that line the small vasculature. We now have good depictions of the heparin-binding site on antithrombin, and of the way in which mutations at this site cause thrombotic disease.
R, Carrell +3 more
openaire +2 more sources
2013
Antithrombin (AT) is a heparin cofactor and a member of the serine protease inhibitor family (serpin). The mature AT molecule is composed of 432 amino acids and it is produced mainly in the liver. Initially, several different AT activities in plasma were reported, leading to the classification of antithrombin in a range from I to IV.
Mirta, Hepner, Vasiliki, Karlaftis
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Antithrombin (AT) is a heparin cofactor and a member of the serine protease inhibitor family (serpin). The mature AT molecule is composed of 432 amino acids and it is produced mainly in the liver. Initially, several different AT activities in plasma were reported, leading to the classification of antithrombin in a range from I to IV.
Mirta, Hepner, Vasiliki, Karlaftis
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SERPINC1 gene mutations in antithrombin deficiency [PDF]
British Journal of Haematology, 2017 Existing evidence suggests that in most cases antithrombin deficiency can be explained by mutations in its gene, SERPINC1. We investigated the molecular background of antithrombin deficiency in a single centre family cohort study.
René Mulder +2 more
exaly +2 more sources
Thrombosis and Haemostasis, 1971
SummaryAn evaluation of the mode of action of antithrombin in the temporary inhibition of purified 3.7 S bovine thrombin was made according to traditional enzyme inhibition theory. Using enzyme clotting activity and concentration of active sites synonymously, it was observed that the binding of antithrombin to thrombin followed a second order reaction ...
Frederick A. Dombrose +2 more
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SummaryAn evaluation of the mode of action of antithrombin in the temporary inhibition of purified 3.7 S bovine thrombin was made according to traditional enzyme inhibition theory. Using enzyme clotting activity and concentration of active sites synonymously, it was observed that the binding of antithrombin to thrombin followed a second order reaction ...
Frederick A. Dombrose +2 more
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Seminars in Thrombosis and Hemostasis, 2007
Angiogenesis is critical for several physiologic and pathophysiologic processes, and several angiogenesis inhibitors are now in clinical trials for the treatment of cancer. Antithrombin is a member of the serpin family of proteins and functions as an inhibitor of thrombin and other enzymes involved in the clotting cascade. While studying the inhibition
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Angiogenesis is critical for several physiologic and pathophysiologic processes, and several angiogenesis inhibitors are now in clinical trials for the treatment of cancer. Antithrombin is a member of the serpin family of proteins and functions as an inhibitor of thrombin and other enzymes involved in the clotting cascade. While studying the inhibition
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Isoform composition of antithrombin in a covalent antithrombin–heparin complex
Biochemical and Biophysical Research Communications, 2003Antithrombin (AT) circulates in two isoforms, alpha- (90-95%) and beta-AT (5-10%). AT inhibits clotting factors such as thrombin and factor Xa, a reaction catalyzed by heparin. Heparin has been used in many clinical situations but suffers from limitations such as a short intravenous half-life, bleeding risk, and the inability to inhibit thrombin bound ...
Anthony K C, Chan +3 more
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Antithrombin and Heparin Antithrombin Patterns in Pre-thrombosis and Thrombosis
American Journal of Clinical Pathology, 1976An antithrombin assay (AA) and an antithrombin assay modified by the addition of heparin (H-AA) were performed using sera from healthy subjects, patients predisposed to thrombosis, and patients with thromboembolic disease. Characteristic AA, and H-AA patterns were found in each group.
I, Innerfield +4 more
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Antiplatelet and antithrombin therapy
Coronary Artery Disease, 1994The contemporary pharmacologic treatment of acute myocardial infarction (AMI) includes reperfusion via a thrombolytic agent as well as adjunctive therapy with aspirin and heparin (1). Despite the advances made, current management is limited by the fact that infarct-related artery patency is achieved in only 60–80% of patients at 90 min and Thrombolysis
A, Fernández-Ortiz +2 more
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Platelet antithrombin activity
Thrombosis Research, 1980Abstract Platelets were studied for the presence of antithrombin (thrombin amidolytic inhibitory) activity. Platelet rich plasma contained more antithrombin activity than platelet poor plasma. This activity could be washed from a platelet pellet. Antithrombin activity increased on sonication of platelets but not following aggregation.
E E, Czapek, H C, Kwaan
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JAMA: The Journal of the American Medical Association, 1978
To the Editor.— In a recent letter to the editor, Rodger L. Bick, MD, commented on methods of assay of antithrombin III (239:296, 1978), pointing out several drawbacks to the use of synthetic chromogenic substrates in such assays. His comments were prompted by an article in MEDICAL NEWS (238:1005, 1977) in which we reported that these peptides were ...
H L, Messmore, J, Fareed
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To the Editor.— In a recent letter to the editor, Rodger L. Bick, MD, commented on methods of assay of antithrombin III (239:296, 1978), pointing out several drawbacks to the use of synthetic chromogenic substrates in such assays. His comments were prompted by an article in MEDICAL NEWS (238:1005, 1977) in which we reported that these peptides were ...
H L, Messmore, J, Fareed
openaire +2 more sources