| Abstract: | Fragment D from a 4-hour plasminolysate of human fibrinogen was chromatographed on DEAE-cellulose and a nearly homogeneous subfraction obtained. It migrated as a single band in dodecylsulfate gel electrophoresis. Reduction yielded three peptide chains with approximate molecular weights of 45000, 295000 and 13000 as estimated from the electrophoretic migration rate in dodecylsulfate acrylamide gels. From these data the molecular weight of the Fragment D subfraction was calculated to be ca. 87500. The S-carboxymethylated peptide chains were separated by chromatography on DEAE-cellulose. They were correlated electrophoretically and their amino acid composition was determined. The peptide chains of molecular weight 45000 and 29500 showed a chromatographic microheterogeneity. The subfractions of these two chains, however, were not distinguished by their electrophoretic mobility in dodecylsulfate acry lamide gels and showed only insignificant differences in their amino acid composition. |
