Chain pairs in the crosslinking of fibrin

Abstract After sultifolysis, enzymatically crosslinked fibrin yields fragments which are different from those obtainable from non-crosslinked material. The α and γ chains of the latter disappear almost entirely and crosslinking bands appear which move slower in electrophoresis. Prominent among these is one with the mobility calculated for an α-γ hybrid chain dimeric combination. The β chain of fibrin appears to be unaffected by crosslinking.