Human prothrombin activation.

摘要: Human prothrombin has been purified from American Red Cross Factor IX concentrates. Studies of the activation human with use sodium dodecyl sulfate electrophoretic analysis products indicated that is similar to bovine activation. Molecular weight and intermediated by co-electrophoresis its intermediates resulted in molecular weights 70,000 for prothrombin, 51,000 intermediate 1, 41,000 2, 23,000 3, 13,000 4. Amino acid compositions are those intermediates. NH2-terminal sequence studies intermediates, alpha-thrombin A B chains placed parent molecule as described system. Intermediate 3 1 COOH-terminal segment zymogen. 4 1. 2', immediate precursor alpha-thrombin, In general, a high degree homology primary structure was observed between The sequences 2' chain identical. However, isolated manner identical used isolation 2 homologous beginning residue 14.