Abstract
Cold-insoluble globulin (CIg) was prepared from rat plasma by means of heat-defibrinogenation at 56°C for 4 min, salting-out at 25 % saturation of ammonium sulfate, ion-exchange chromatography on DEAE-cellulose and affinity chromatography using fibrinmonomer-Sepharose. Sodium dodecyl sulfate polyacrylamide gel electrophoresis run on the purified rat CIg showed a major 4.4 × 10 5 dalton polypeptide and a minor closely migrating doublet with a molecular weight half as large as the major one under unreducing conditions. When the sample was reduced, a doublet with an approximate molecular weight of 2.2 × 10 5 was noted. Other characteristics and properties described on human and bovine CIg's were found in the purified rat CIg as well, including electrophoretic mobility and immunological cross-reactivity with CIg of other species. The overall recovery and purification in a typical run were 33 % and 68-fold, respectively.
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