| pubmed-article:3187961 | pubmed:abstractText | Human brain tissue factor apoprotein was recently purified to homogeneity in this laboratory by affinity chromatography utilizing factor VII bound to immobilized anti-factor VII (Anal Biochem 165, 365-370, 1987). A potent polyclonal anti-tissue factor antibody has now been raised to the purified apoprotein. Immunostaining of purified tissue factor with this polyclonal IgG yielded a single major band with an apparent molecular weight of 47,000, which corresponds to the mobility on SDS-PAGE of tissue factor apoprotein. Immunostaining of a crude Triton extract of brain tissue yielded two additional bands, with apparent molecular weights of 54,000 and 40,000 Da. An anti-tissue factor IgG was coupled to Affi-Gel-15 to prepare an immunoadsorbant column. The two additional proteins in the crude Triton extract recognized by Western blotting did not bind to the column. This permitted its use to develop a simple, efficient technique for purification of human tissue factor apoprotein. | lld:pubmed |
