The minor form alpha' chain from lamprey fibrinogen is rapidly crosslinked during clotting.

Lampreys have two genes for the alpha chains of fibrinogen, the second of which encodes a minor form with a carboxyl-terminal domain homologous to the carboxyl-terminal domains of beta and gamma chains. Initially, we referred to the alternative chain as alpha-II; we now use the designation alpha' in order to facilitate reference to crosslinked dimers. Antisera raised to synthetic peptides based on the cDNA sequence confirmed that the alpha' chain was present in fibrinogen prepared directly from plasma. The same antibodies were used to determine the size and properties of the carboxyl-terminal domain after its release by mild tryptic digestion, a fragment of apparent molecular weight 35,000-40,000 being produced. Unlike fragment D generated in the same digestions, the alpha' fragment did not bind to Gly-Pro-Arg or Gly-Val-Arg peptide affinity columns. During clotting under conditions where factor XIII is active, the alpha' chains became crosslinked very much more rapidly than ordinary alpha chains, the principal product being an apparent dimer, but smaller amounts of higher multimers being detectable. The crosslinking was inhibited by various amines, as well as by peptides that prevent polymerization.