The cold-insoluble globulin of human plasma. I. Purification, primary characterization, and relationship to fibrinogen and other cold-insoluble fraction components.

摘要: Abstract The cold-insoluble globulin (CI-globulin) of human plasma has been highly purified. Starting with Fraction I-1, or cryoprecipitate, 2.1 m glycine fractionation (15°) precipitated mainly fibrinogen; concentration supernatant CI-globulin-enriched material (16% ethanol, -4°) was carried out prior to final purification by chromatography on di-ethylaminoethylcellulose. Chromatographically purified CI-globulin contained no detectable fibrinogen and homogeneous upon ultracentrifugation (s20,w0 = 12.3 S); only trace amounts NH2-terminal amino acids were detectable. migrated as a fast β-globulin in agarose gel cellulose acetate strip electrophoresis. In immunoelectrophoretic experiments, formed single precipitin arc against an anti-CI-globulin serum. There lipid, fibrin-stabilizing factor (Factor XIII), anti-hemophilic Factor B IX), plasminogen, plasmin, thrombin inhibitory activity; low levels A VIII) activity present. evidence any alteration the electrophoretic, ultracentrifugal, characteristics following treatment heating 56° for 5 min. level, estimated antigen-antibody crossed electrophoresis, 0.33 g per liter (range 0.26 0.38, n 12). level serum, 0.20 0.14 0.30, 11), consistently lower (19 52%), presumably attributable incorporation occlusion fibrin clot. After removal cryoprecipitate Cohn I, reduced 59 79%, respectively.