A simple purification of human Factor X using a high affinity monoclonal antibody immunoadsorbant
- 1 May 1985
- journal article
- research article
- Published by Elsevier in Thrombosis Research
- Vol. 38 (4), 417-424
- https://doi.org/10.1016/0049-3848(85)90140-9
Abstract
No abstract availableThis publication has 19 references indexed in Scilit:
- Human hepatoma cells secrete single chain factor X, prothrombin, and antithrombin IIIBlood, 1984
- Blood coagulation factor X mRNA encodes a single polypeptide chain containing a prepro leader sequenceNucleic Acids Research, 1984
- Immunoaffinity purification of bovine factor VIIBlood, 1984
- Thrombin proteolysis of purified factor viii procoagulant protein: correlation of activation with generation of a specific polypeptideBlood, 1983
- Monoclonal antibodies selective for the functional states of bovine factor V and factor VaThrombosis Research, 1982
- Monoclonal antibodies: Purification, fragmentation and application to structural and functional studies of class I MHC antigensJournal of Immunological Methods, 1982
- Monoclonal antibodies to porcine factor VIII coagulant and their use in the isolation of active coagulant proteinBlood, 1982
- Protein and cell membrane iodinations with a sparingly soluble chloroamide, 1,3,4,6-tetrachloro-3a,6a-diphenylglycolurilBiochemical and Biophysical Research Communications, 1978
- A simplified method for cyanogen bromide activation of agarose for affinity chromatographyAnalytical Biochemistry, 1974
- Simultaneous Purification of Bovine Prothrombin and Factor XJournal of Biological Chemistry, 1973