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References range may vary with age, sex, race, pregnancy, [10] diet, use of prescribed or herbal drugs and stress. Reference ranges often depend on the analytical method used, for reasons such as inaccuracy, lack of standardisation, lack of certified reference material and differing antibody reactivity. [11]
Native heparin is a polymer with a molecular weight ranging from 3 to 30 kDa, although the average molecular weight of most commercial heparin preparations is in the range of 12 to 15 kDa. [60] Heparin is a member of the glycosaminoglycan family of carbohydrates (which includes the closely related molecule heparan sulfate ) and consists of a ...
Low molecular weight heparin at full weight based dosing is effective; however, measurements of peak anti-Xa levels may not reflect anticoagulant effect. Vitamin K antagonists, and direct oral anticoagulants, including anti-Xa inhibitors and thrombin inhibitors have also been used, though data is limited. [6]
Direct factor Xa inhibitors (xabans) are anticoagulants (blood thinning drugs), used to both treat and prevent blood clots in veins, and prevent stroke and embolism in people with atrial fibrillation (AF).
The first crystal structure of human factor Xa was deposited in May 1993. To date, 191 crystal structures of factor Xa with various inhibitors have been deposited in the protein data bank. The active site of factor Xa is divided into four subpockets as S1, S2, S3 and S4. The S1 subpocket determines the major component of selectivity and binding.
Apart from using unfractionated heparin instead, it may be possible to reduce the dose and/or monitor the anti-Xa activity to guide treatment. [ 3 ] The most common side effects include bleeding, which could be severe or even fatal, allergic reactions, injection site reactions, and increases in liver enzyme tests, usually without symptoms. [ 13 ]
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Antithrombin (AT) is a small glycoprotein that inactivates several enzymes of the coagulation system. It is a 464-amino-acid protein produced by the liver.It contains three disulfide bonds and a total of four possible glycosylation sites. α-Antithrombin is the dominant form of antithrombin found in blood plasma and has an oligosaccharide occupying each of its four glycosylation sites.