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. A single glycosylation site remains consistently un-occupied in the minor form of antithrombin, β-antithrombin.[5] Its activity is increased manyfold by the anticoagulant drug heparin, which enhances the binding of antithrombin to factor IIa (thrombin) and factor Xa.[6]
- ^ a b c GRCh38: Ensembl release 89: ENSG00000117601 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000026715 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ Bjork I, Olson, JE (1997). Antithrombin, A bloody important serpin (in Chemistry and Biology of Serpins). Plenum Press. pp. 17–33. ISBN 978-0-306-45698-5.
- ^ Finley A, Greenberg C (June 2013). "Review article: heparin sensitivity and resistance: management during cardiopulmonary bypass". Anesthesia and Analgesia. 116 (6): 1210–1222. doi:10.1213/ANE.0b013e31827e4e62. PMID 23408671. S2CID 22500786.