Sumita Choudhury, William E Plautz, Cosette Zacarias, Rinku Majumder
{"title":"Mini-review on \"A novel one-step purification of mouse factor IX\".","authors":"Sumita Choudhury, William E Plautz, Cosette Zacarias, Rinku Majumder","doi":"10.29245/2572-9411/2016/2.1031","DOIUrl":null,"url":null,"abstract":"Factor IX (FIX) is a 70-kDa, single-chain, vitamin K-dependent glycoprotein present in trace amounts (~95 nM) in blood plasma1,2. FIX is synthesized as a zymogen that is converted to a serine protease, FIXa, by the activated form of factor XI3,4. FIXa has a central function in the intrinsic pathway of blood coagulation, in that it acts as an activator of factor X (FX), directly upstream of the common pathway1,5. Upon activation, FXa concomitantly converts prothrombin to thrombin to initiate the formation of the fibrin lattice6,7.","PeriodicalId":91764,"journal":{"name":"Journal of rare diseases research & treatment","volume":"43 1","pages":"8-10"},"PeriodicalIF":0.0000,"publicationDate":"2016-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of rare diseases research & treatment","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.29245/2572-9411/2016/2.1031","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0
Abstract
Factor IX (FIX) is a 70-kDa, single-chain, vitamin K-dependent glycoprotein present in trace amounts (~95 nM) in blood plasma1,2. FIX is synthesized as a zymogen that is converted to a serine protease, FIXa, by the activated form of factor XI3,4. FIXa has a central function in the intrinsic pathway of blood coagulation, in that it acts as an activator of factor X (FX), directly upstream of the common pathway1,5. Upon activation, FXa concomitantly converts prothrombin to thrombin to initiate the formation of the fibrin lattice6,7.