title: Research on PEGylation of porcine prothrombin for improving biostability and reducing animal immunogenicity.
abstract: Prothrombin is a vitamin K-dependent serine protease and plays pivotal roles in both procoagulant and anticoagulant pathway of hemostasis. In this study, prothrombin purified from porcine plasma was modified through PEGylation at N-terminal residue using 40 kDa PEG-phenyl-isothiocyanate (PIT-PEG40K). The monoPEGylated prothrombin enhanced biostability and remarkably prolonged circulating half-life in mice as compared with that of the nonmodified prothrombin. Moreover, the immunogenicity of PEGylated prothrombin in mice is significantly decreased compared to nonmodified prothrombin. These studies demonstrated the feasibility of PEGylating prothrombin as a promising way for the development of new prothrombin drugs.
authors.affiliation: College of Environment and Urban Construction, Wuhan Textile University, Wuhan 430073, PR China.
authors.forename: Jian-Gang
authors.initials: JG
authors.lastname: Zhou
authors.forename: Ying-Ming
authors.initials: YM
authors.lastname: Chen
mesh_terms: D000818:Animals; D004355:Drug Stability; D055261:Immunogenetic Phenomena / Q000187:drug effects; D051379:Mice; D011092:Polyethylene Glycols / Q000737:chemistry / Q000494:pharmacology; D011516:Prothrombin / Q000737:chemistry* / Q000494:pharmacology; D013552:Swine
chemical_list: D011092:Polyethylene Glycols; D011516:Prothrombin