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• W1530699966 abstract "Human coagulation factor IX was purified by two ion-exchange chromatographies on DEAE-Sephadex A-50, heparin-Sepharose chromatography, hydroxyapatite chromatography and immuno-adsorbent technique. Factor IX was homogeneous by ordinary and sodium dodecylsulphate disc electrophoresis, N-terminal amino acid analyses and ultracentrifugation and by immunological criteria. The following molecular data were observed: 1 Sedimentation equilibrium indicated a molecular weight of 66 100 and sedimentation velocity gave S20, w= 3.97 S. A partial specific volume of v̄= 0.712 ml/g was calculated from the amino acid and carbohydrate composition. 2 Sodium dodecylsulphate disc gel electrophoresis suggested a molecular weight of 65 000. 3 Gel filtration indicated a Stokes radius of 4.08 nm, and ‘a molecular weight’ of 72 000, as well as a diffusion coefficient D20, w= 5.15 × 10−7 cm2 s−1 and a frictional ratio f/f0= 1.54. 4 Tyrosine was the N-terminal amino acid. The amino acid composition is described. Factor IX contained approximately 17.5% carbohydrate, which includes 4.7% hexose, 6.8%N-acetylhexos-amine and 6% sialic acid. 5 Microheterogeneity of pure factor IX was demonstrated by isoelectric focusing. The isoelectric points of the major components lay within the range of pH 4.0 to 4.6. 6 The antibody raised in rabbits against the pure factor IX did not react with the other vitamin-K-dependent coagulation factors measured by coagulation factor assays or immunodiffusion in gels." @default.
• W1530699966 created "2016-06-24" @default.
• W1530699966 creator A5089535637 @default.
• W1530699966 date "1976-12-01" @default.
• W1530699966 modified "2023-10-18" @default.
• W1530699966 title "Human Coagulation Factor IX. Isolation and Characterization" @default.
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• W1530699966 doi "https://doi.org/10.1111/j.1432-1033.1976.tb11100.x" @default.
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