title: [High purification of human thrombin].
abstract: A highly purified human thrombin was prepared from plasma. The procedure involved the adsorption of prothrombin from human plasma by barium chloride and precipitation by using ammonium sulfate. The partially purified prothrombin was activated by tissue thromboplastin and followed by chromatography on Amberllte and SP-Sephadex. The purified enzyme is homogeneous on SDS-PAGE and has a specific activity toward fibrinogen of 2000 NIH U/mg. The recovery is about 30% approximately 40%. This highly purified human thrombin can be used as a tool enzyme in the downstream procedure of fused recombinant proteins expressed by genetic engineering.
authors.affiliation: Institute of Basic Medical Sciences, CRRC, Beijing.
authors.forename: J
authors.initials: J
authors.lastname: Zhong
authors.forename: W
authors.initials: W
authors.lastname: Yin
authors.forename: Y
authors.initials: Y
authors.lastname: Lin
authors.forename: Y
authors.initials: Y
authors.lastname: Liu
authors.forename: S
authors.initials: S
authors.lastname: Lu
mesh_terms: D000595:Amino Acid Sequence; D006801:Humans; D008969:Molecular Sequence Data; D010949:Plasma / Q000201:enzymology*; D013917:Thrombin / Q000737:chemistry / Q000302:isolation & purification*
chemical_list: D013917:Thrombin