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Digestion of fibrinogen with a number of proteolytic enzymes yields a series of large fragments with protein-like structure and a substantial amount of peptidic material. Some of the peptides released possess biological activity, therefore, the study of their formation and properties may be of clinical interest. In the present investigations human or bovine fibrinogen was digested by either plasmin or trypsin. Approximately 35% of the fibrinogen molecule is removed as peptides with either enzyme and these are well divided into two groups: 1. large peptides of 15,000 to 40,000 MW and 2. small peptides of less than 10,000 MW. The distribution of material between these groups is approximately the same with either enzyme and with bovine or human fibrinogen, however, the plasmic peptides in either group are larger than the tryptic ones. All the large peptides are derived from the approximately 40,000 MW C-terminal portion of the α-chain. In this segment, according to the sequence of the human α-chain, there are 33 bonds theoretically susceptible to either plasmin or trypsin. Of these, only 3 are attacked at a fast rate by plasmin in the native molecule, resulting in the appearance of peptide segments of 40,000, 32,000 and 26,000 MW. The first two are short lived, reach only about 25% of the stoichiometric amount, and are converted into the last one, which accumulates as a fairly stable end product. Trypsin digestion of the latter involves again 3 susceptible bonds and through an intermediate of 17,000 MW results in 2 fragments, one of 10,000 and another of 7,000 MW. The restricted cleavage of susceptible bonds in these fragments, their intrinsic viscosity and its increase in denaturing media, suggest that these peptides possess a fairly compact structure, i.e., they are not in the random coil state as hitherto suggested.

Studies Of The Peptide Fractions Derived From Fibrinogen By Digestion With Trypsin Or Plasmin