Abstract
Polymerization of purified fragment X preparations, obtained from a late stage 2 plasmin digest of fibrinogen, was studied by turbidimetry and electron microscopy. The thrombin-induced polymerization of fragment X caused a rapid increase in turbidity followed by a slow decrease. The initial turbidity increase of fragment X polymers was considerably greater than that of normal fibrin. Electron microscopy carried out at different time points in the reaction revealed that initially there was a great deal of lateral aggregation of fragment X fibers. At later times, electron microscopy showed that there was more dispersal or disruption of the fibers, corresponding to the decrease in turbidity. The slow decrease in turbidity was apparently caused by the rearrangement and/or splitting apart of fragment X fibers, starting from a state similar to a very coarse clot, with much aggregation of fibers, to a delicate meshwork, similar to a fine clot. These changes in clot and fiber structure may result from cleavages partly in the carboxy-terminal region of the γ chains and the amino-terminal region of the Bβ chain of fragment X or the influence of other non-clottable fragments present in these preparations.
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