Purification and characterization of ostrich prothrombin.

作者: Carminita Frost , Ryno Naudé , Willem Oelofsen , Koji Muramoto , Takako Naganuma

DOI: 10.1016/S1357-2725(00)00062-5

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摘要: Abstract The work focused on the penultimate enzyme, prothrombin, in coagulation cascade. Prothrombin was purified and characterized from ostrich plasma. results obtained contribute to a better understanding of blood evolution prothrombin plasma by barium chloride precipitation, ammonium sulfate fractionation, DEAE-cellulose Cu2+-chelate Sepharose chromatography. Ostrich exhibited Mr 72 800 pI 6.9 using SDS-PAGE PAG-isoelectrofocusing, respectively. N-terminal sequence showed 78 87% identity with human bovine, cDNA isolated liver predicted amino acid compared those other species. shares chicken (84%), (60%), bovine (59%), rat mouse (59%) hagfish (50%) suggesting common function these vertebrates. Amino identities indicate that thrombin β-chain (62%) propeptide-Gla (75%) domains are regions most constrained for functions vertebrate prothrombins. therefore, shows similarity structure

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