抄録
Cold-insoluble globulin (CIg) was prepared from rat glasma by means of heat-defibrinogenstion at 56°C for 4min, salting-out at 25% saturation of ammonium sulfate, ion-exchange chromatography on DEAE-cellulose and affinity chromatography using fibrinmonomer-Sepharose. SDS polyacrylamide gel electrophoresis run on the purified rat CIg chowed a major 4.4×105 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 2.2×105 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.
