Results 161 to 170 of about 1,671 (202)
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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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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
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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
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British Journal of Haematology, 1984
SummaryAntithrombin III (AT‐III) heparin cofactor activity and its antigen levels have been determined in 106 plasma samples from 42 term and preterm neonates. In contrast to healthy adult controls, a reduced activity/antigen (act/ag) ratio (ranging from 0‐26 to 0‐86) was observed in 90% of the samples and was independent of the state of health of the ...
Peters, M. +5 more
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SummaryAntithrombin III (AT‐III) heparin cofactor activity and its antigen levels have been determined in 106 plasma samples from 42 term and preterm neonates. In contrast to healthy adult controls, a reduced activity/antigen (act/ag) ratio (ranging from 0‐26 to 0‐86) was observed in 90% of the samples and was independent of the state of health of the ...
Peters, M. +5 more
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Hirudins: Antithrombin Anticoagulants
Annals of Pharmacotherapy, 1992OBJECTIVE: To review the chemistry, pharmacology, available clinical data, and adverse effects of the hirudin anticoagulants. DATA SOURCES: A MEDLINE search and a review of recent scientific abstracts was conducted to identify pertinent literature. STUDY SELECTION: Focus was placed on studies conducted in humans.
K A, Stringer, J, Lindenfeld
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Thrombosis Research, 1982
Plasma from two different thrombophilic families with functional inherited antithrombin III deficiency, i.e., with low antithrombin III activity but normal immunoreactive antithrombin III concentration, were investigated simultaneously in the same laboratory.
P J, Sørensen +5 more
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Plasma from two different thrombophilic families with functional inherited antithrombin III deficiency, i.e., with low antithrombin III activity but normal immunoreactive antithrombin III concentration, were investigated simultaneously in the same laboratory.
P J, Sørensen +5 more
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Commercial Antithrombin Concentrate Contains Inactive L-forms of Antithrombin
Thrombosis and Haemostasis, 1997SummaryThe preparation of antithrombin concentrate for clinical use requires a viral inactivation step. In most commercial preparations this is achieved by heat pasteurisation. This process would be expected to alter the conformation of antithrombin from the active native species to an inactive latent (L-form) state (1, 2).
W S, Chang, P L, Harper
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Hematology/Oncology Clinics of North America, 1992
The general characteristics of antithrombin III (AT III) concentrates available in the United States are described in this article. The effectiveness of AT III concentrates in the prevention and treatment of thrombotic episodes in patients with hereditary AT III deficiency are summarized, and the use of this product in various conditions with acquired ...
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The general characteristics of antithrombin III (AT III) concentrates available in the United States are described in this article. The effectiveness of AT III concentrates in the prevention and treatment of thrombotic episodes in patients with hereditary AT III deficiency are summarized, and the use of this product in various conditions with acquired ...
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Blood Reviews, 1988
A moderate reduction of plasma antithrombin activity is an uncommon but clinically important cause of severe thromboembolic disease. In recent years the molecule responsible for the major part of this activity (antithrombin III) has been extensively characterised and the mode of inheritance of familial deficiencies worked out.
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A moderate reduction of plasma antithrombin activity is an uncommon but clinically important cause of severe thromboembolic disease. In recent years the molecule responsible for the major part of this activity (antithrombin III) has been extensively characterised and the mode of inheritance of familial deficiencies worked out.
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